Atomistry » Magnesium » PDB 5h2f-5hi8 » 5han
Atomistry »
  Magnesium »
    PDB 5h2f-5hi8 »
      5han »

Magnesium in PDB 5han: Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)

Enzymatic activity of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)

All present enzymatic activity of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound):
4.1.1.39;

Protein crystallography data

The structure of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound), PDB code: 5han was solved by M.A.Arbing, J.G.Leong, V.A.Varaljay, S.Satagopan, J.A.North, F.R.Tabita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.04
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 75.880, 110.370, 167.360, 89.87, 101.70, 105.00
R / Rfree (%) 19.7 / 23.7

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Magnesium atom in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) (pdb code 5han). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound), PDB code: 5han:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 1 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:30.6
occ:1.00
HO3 A:CAP500 1.4 35.1 1.0
OE1 A:GLU195 1.9 27.6 1.0
OQ2 A:KCX192 2.1 24.2 1.0
OD1 A:ASP194 2.1 41.3 1.0
O6 A:CAP500 2.1 32.2 1.0
O3 A:CAP500 2.2 34.8 1.0
O2 A:CAP500 2.2 42.2 1.0
HO2 A:CAP500 2.8 41.1 1.0
C A:CAP500 2.8 35.5 1.0
C2 A:CAP500 2.8 38.8 1.0
H A:GLU195 2.8 31.9 1.0
HD21 B:ASN112 2.8 37.7 1.0
HZ3 A:LYS169 3.0 61.6 1.0
C3 A:CAP500 3.0 40.5 1.0
CD A:GLU195 3.0 36.8 1.0
HZ1 A:LYS169 3.1 61.4 1.0
CX A:KCX192 3.2 27.3 1.0
HZ2 A:LYS167 3.2 38.0 1.0
CG A:ASP194 3.3 42.2 1.0
HZ2 A:LYS169 3.3 61.1 1.0
HE2 A:HIS288 3.3 30.3 1.0
NZ A:LYS169 3.3 61.3 1.0
H3 A:CAP500 3.4 41.5 1.0
OQ1 A:KCX192 3.5 28.2 1.0
HG21 A:ILE165 3.5 33.8 1.0
HA A:ASP194 3.5 31.5 1.0
ND2 B:ASN112 3.6 37.8 1.0
OE2 A:GLU195 3.6 33.7 1.0
HD22 B:ASN112 3.6 37.9 1.0
N A:GLU195 3.8 32.6 1.0
HB3 A:GLU195 3.9 34.6 1.0
NE2 A:HIS288 3.9 29.1 1.0
OD2 A:ASP194 4.0 47.3 1.0
O7 A:CAP500 4.0 35.7 1.0
NZ A:LYS167 4.0 39.0 1.0
HE1 A:HIS288 4.1 30.2 1.0
HZ1 A:LYS167 4.1 38.9 1.0
CG A:GLU195 4.2 35.0 1.0
HZ3 A:LYS167 4.2 40.4 1.0
CA A:ASP194 4.2 30.5 1.0
C1 A:CAP500 4.3 33.6 1.0
C4 A:CAP500 4.3 42.4 1.0
CB A:ASP194 4.3 28.9 1.0
CE1 A:HIS288 4.3 28.6 1.0
NZ A:KCX192 4.4 26.6 1.0
CB A:GLU195 4.4 34.3 1.0
H4 A:CAP500 4.5 42.4 1.0
C A:ASP194 4.5 34.9 1.0
HG12 A:ILE165 4.5 33.6 1.0
HD3 A:PRO196 4.5 31.9 1.0
CG2 A:ILE165 4.6 33.3 1.0
H52 A:CAP500 4.6 40.2 1.0
H12 A:CAP500 4.6 33.3 1.0
O1 A:CAP500 4.7 32.6 1.0
CA A:GLU195 4.7 32.8 1.0
HG3 A:GLU195 4.7 33.0 1.0
CG B:ASN112 4.7 44.1 1.0
CE A:LYS169 4.8 57.9 1.0
HD13 A:ILE165 4.8 29.0 1.0
C5 A:CAP500 4.8 41.3 1.0
H51 A:CAP500 4.8 42.0 1.0
HG3 A:LYS169 4.8 45.6 1.0
H11 A:CAP500 4.9 34.5 1.0
HG22 A:ILE165 4.9 33.6 1.0
CD2 A:HIS288 4.9 29.7 1.0
HG2 A:GLU195 4.9 35.0 1.0
HB3 A:ASP194 5.0 29.0 1.0
O B:HOH683 5.0 38.5 1.0

Magnesium binding site 2 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 2 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:36.6
occ:1.00
HO3 B:CAP500 1.6 31.1 1.0
OD1 B:ASP194 1.9 29.4 1.0
OQ2 B:KCX192 1.9 31.6 1.0
OE1 B:GLU195 1.9 34.3 1.0
O6 B:CAP500 2.2 34.4 1.0
O2 B:CAP500 2.2 46.8 1.0
O3 B:CAP500 2.4 30.7 1.0
HO2 B:CAP500 2.7 48.0 1.0
H B:GLU195 2.7 34.7 1.0
C2 B:CAP500 2.8 36.4 1.0
C B:CAP500 2.9 33.1 1.0
CX B:KCX192 3.0 31.9 1.0
CD B:GLU195 3.1 52.1 1.0
HZ2 B:LYS167 3.1 32.2 1.0
HD21 A:ASN112 3.1 38.3 1.0
CG B:ASP194 3.1 32.8 1.0
C3 B:CAP500 3.1 32.9 1.0
OQ1 B:KCX192 3.3 31.8 1.0
HZ3 B:LYS169 3.3 38.2 1.0
HZ2 B:LYS169 3.4 38.6 1.0
HA B:ASP194 3.4 30.7 1.0
HG21 B:ILE165 3.4 24.9 1.0
H3 B:CAP500 3.5 34.1 1.0
OE2 B:GLU195 3.6 41.7 1.0
NZ B:LYS169 3.7 39.4 1.0
HZ1 B:LYS169 3.7 40.4 1.0
N B:GLU195 3.7 33.9 1.0
HD22 A:ASN112 3.7 38.6 1.0
ND2 A:ASN112 3.8 38.3 1.0
OD2 B:ASP194 3.8 38.0 1.0
NZ B:LYS167 3.9 33.7 1.0
HB3 B:GLU195 3.9 34.5 1.0
HZ1 B:LYS167 4.0 35.7 1.0
NE2 B:HIS288 4.0 33.6 1.0
O7 B:CAP500 4.1 32.0 1.0
CA B:ASP194 4.1 29.2 1.0
HZ3 B:LYS167 4.1 34.2 1.0
CB B:ASP194 4.2 30.7 1.0
NZ B:KCX192 4.2 31.2 1.0
CG B:GLU195 4.2 47.6 1.0
C1 B:CAP500 4.2 38.0 1.0
HD3 B:PRO196 4.3 35.6 1.0
HE1 B:HIS288 4.3 32.0 1.0
C B:ASP194 4.4 35.4 1.0
CB B:GLU195 4.4 33.9 1.0
CG2 B:ILE165 4.4 27.6 1.0
C4 B:CAP500 4.5 31.2 1.0
CE1 B:HIS288 4.5 32.2 1.0
H12 B:CAP500 4.6 36.2 1.0
O1 B:CAP500 4.6 37.7 1.0
HG22 B:ILE165 4.6 27.4 1.0
H4 B:CAP500 4.6 31.1 1.0
CA B:GLU195 4.7 32.5 1.0
HG3 B:LYS169 4.7 35.6 1.0
H52 B:CAP500 4.8 32.9 1.0
HG3 B:GLU195 4.8 48.6 1.0
HB3 B:ASP194 4.8 29.6 1.0
O A:HOH691 4.8 39.9 1.0
HB2 B:ASP194 4.8 31.1 1.0
H11 B:CAP500 4.9 39.5 1.0
O A:HOH744 4.9 40.4 1.0
HG2 B:GLU195 4.9 47.4 1.0
HG23 B:ILE165 5.0 27.6 1.0

Magnesium binding site 3 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 3 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg501

b:34.4
occ:1.00
HO3 C:CAP500 1.5 34.9 1.0
OD1 C:ASP194 1.9 29.8 1.0
OE1 C:GLU195 2.0 36.9 1.0
O6 C:CAP500 2.1 32.5 1.0
O2 C:CAP500 2.1 42.1 1.0
OQ2 C:KCX192 2.1 33.1 1.0
O3 C:CAP500 2.3 37.3 1.0
HO2 C:CAP500 2.7 42.3 1.0
C2 C:CAP500 2.7 38.6 1.0
C C:CAP500 2.7 32.7 1.0
H C:GLU195 2.9 34.2 1.0
HD21 D:ASN112 3.0 47.9 1.0
HZ2 C:LYS167 3.0 38.0 1.0
C3 C:CAP500 3.0 39.0 1.0
CG C:ASP194 3.1 35.9 1.0
CD C:GLU195 3.1 43.4 1.0
CX C:KCX192 3.2 33.8 1.0
HG21 C:ILE165 3.3 30.6 1.0
HZ3 C:LYS169 3.4 54.0 1.0
OQ1 C:KCX192 3.4 38.3 1.0
HZ2 C:LYS169 3.4 54.1 1.0
H3 C:CAP500 3.4 39.4 1.0
HA C:ASP194 3.5 32.1 1.0
OE2 C:GLU195 3.7 37.3 1.0
HZ1 C:LYS169 3.7 54.0 1.0
NZ C:LYS169 3.7 53.9 1.0
HD22 D:ASN112 3.7 47.7 1.0
ND2 D:ASN112 3.7 47.7 1.0
OD2 C:ASP194 3.7 42.1 1.0
NZ C:LYS167 3.8 40.1 1.0
N C:GLU195 3.8 33.6 1.0
HZ1 C:LYS167 4.0 40.9 1.0
O7 C:CAP500 4.0 33.7 1.0
HB3 C:GLU195 4.0 36.1 1.0
NE2 C:HIS288 4.1 32.3 1.0
HZ3 C:LYS167 4.1 40.5 1.0
C1 C:CAP500 4.1 39.1 1.0
CA C:ASP194 4.2 32.9 1.0
CB C:ASP194 4.2 31.5 1.0
NZ C:KCX192 4.3 32.0 1.0
HG12 C:ILE165 4.3 35.5 1.0
HE1 C:HIS288 4.3 32.3 1.0
CG C:GLU195 4.3 41.0 1.0
C4 C:CAP500 4.4 39.6 1.0
CG2 C:ILE165 4.4 31.2 1.0
HD3 C:PRO196 4.4 33.2 1.0
C C:ASP194 4.5 38.6 1.0
H4 C:CAP500 4.5 40.6 1.0
CB C:GLU195 4.5 35.1 1.0
CE1 C:HIS288 4.5 31.7 1.0
O1 C:CAP500 4.5 35.9 1.0
H11 C:CAP500 4.6 40.0 1.0
HG22 C:ILE165 4.7 31.4 1.0
H52 C:CAP500 4.7 34.3 1.0
H12 C:CAP500 4.8 39.6 1.0
HG3 C:LYS169 4.8 32.3 1.0
CA C:GLU195 4.8 33.5 1.0
HB3 C:ASP194 4.8 28.7 1.0
HD13 C:ILE165 4.8 38.9 1.0
HG23 C:ILE165 4.8 28.7 1.0
HG3 C:GLU195 4.9 40.5 1.0
HB2 C:ASP194 4.9 30.3 1.0
C5 C:CAP500 4.9 36.1 1.0
CG D:ASN112 4.9 51.7 1.0
H51 C:CAP500 5.0 35.6 1.0
O D:HOH657 5.0 50.5 1.0
HE2 C:LYS167 5.0 29.6 1.0

Magnesium binding site 4 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 4 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg501

b:35.2
occ:1.00
HO3 D:CAP500 1.5 30.4 1.0
OD1 D:ASP194 2.0 32.6 1.0
O2 D:CAP500 2.0 37.2 1.0
OQ2 D:KCX192 2.0 27.6 1.0
OE1 D:GLU195 2.1 37.6 1.0
O6 D:CAP500 2.1 33.4 1.0
O3 D:CAP500 2.3 30.3 1.0
HO2 D:CAP500 2.6 37.2 1.0
C2 D:CAP500 2.7 32.2 1.0
C D:CAP500 2.7 36.3 1.0
H D:GLU195 2.9 33.2 1.0
HZ2 D:LYS167 3.0 39.1 1.0
C3 D:CAP500 3.0 33.4 1.0
HD21 C:ASN112 3.0 34.2 1.0
CX D:KCX192 3.1 32.0 1.0
CG D:ASP194 3.1 33.7 1.0
HG21 D:ILE165 3.2 38.8 1.0
CD D:GLU195 3.2 38.7 1.0
OQ1 D:KCX192 3.3 34.9 1.0
H3 D:CAP500 3.4 34.1 1.0
HZ3 D:LYS169 3.4 39.9 1.0
HE2 D:HIS288 3.5 31.8 1.0
HA D:ASP194 3.5 27.6 1.0
HZ2 D:LYS169 3.5 39.3 1.0
OD2 D:ASP194 3.7 42.0 1.0
HZ1 D:LYS169 3.8 39.2 1.0
NZ D:LYS169 3.8 39.7 1.0
OE2 D:GLU195 3.8 39.6 1.0
HD22 C:ASN112 3.8 35.2 1.0
ND2 C:ASN112 3.8 33.5 1.0
NZ D:LYS167 3.8 41.1 1.0
N D:GLU195 3.9 32.4 1.0
HZ1 D:LYS167 3.9 41.9 1.0
O7 D:CAP500 4.0 31.4 1.0
HB3 D:GLU195 4.0 32.5 1.0
HZ3 D:LYS167 4.0 42.3 1.0
NE2 D:HIS288 4.1 29.6 1.0
C1 D:CAP500 4.1 33.5 1.0
CA D:ASP194 4.2 28.2 1.0
HG12 D:ILE165 4.2 36.5 1.0
CB D:ASP194 4.2 29.6 1.0
NZ D:KCX192 4.3 30.8 1.0
CG2 D:ILE165 4.3 38.2 1.0
C4 D:CAP500 4.3 33.4 1.0
HE1 D:HIS288 4.4 32.0 1.0
CG D:GLU195 4.4 35.9 1.0
HD3 D:PRO196 4.5 36.7 1.0
H12 D:CAP500 4.5 32.0 1.0
O1 D:CAP500 4.5 37.6 1.0
H4 D:CAP500 4.5 34.7 1.0
C D:ASP194 4.5 35.6 1.0
CE1 D:HIS288 4.6 29.9 1.0
CB D:GLU195 4.6 31.7 1.0
HG22 D:ILE165 4.6 38.4 1.0
H52 D:CAP500 4.7 34.1 1.0
H11 D:CAP500 4.7 33.3 1.0
HD13 D:ILE165 4.7 34.9 1.0
HG23 D:ILE165 4.8 37.1 1.0
HG3 D:LYS169 4.8 32.3 1.0
HB3 D:ASP194 4.8 31.0 1.0
CA D:GLU195 4.9 31.4 1.0
HE2 D:LYS167 4.9 43.1 1.0
HB2 D:ASP194 4.9 30.2 1.0
C5 D:CAP500 4.9 34.3 1.0
H51 D:CAP500 4.9 33.3 1.0
HG3 D:GLU195 5.0 37.5 1.0
O C:HOH616 5.0 36.8 1.0

Magnesium binding site 5 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 5 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg501

b:25.7
occ:1.00
HO3 E:CAP500 1.5 31.2 1.0
OE1 E:GLU195 1.9 28.7 1.0
OD1 E:ASP194 2.0 33.9 1.0
OQ2 E:KCX192 2.0 23.6 1.0
O6 E:CAP500 2.1 28.7 1.0
O2 E:CAP500 2.2 27.7 1.0
O3 E:CAP500 2.3 29.8 1.0
H E:GLU195 2.7 28.4 1.0
HO2 E:CAP500 2.7 29.2 1.0
C2 E:CAP500 2.8 30.7 1.0
C E:CAP500 2.8 26.1 1.0
HD21 F:ASN112 2.9 38.3 1.0
CX E:KCX192 3.0 29.0 1.0
CD E:GLU195 3.1 35.4 1.0
C3 E:CAP500 3.1 30.4 1.0
CG E:ASP194 3.1 33.5 1.0
HZ2 E:LYS167 3.2 30.1 1.0
OQ1 E:KCX192 3.3 30.7 1.0
HG21 E:ILE165 3.3 26.1 1.0
HA E:ASP194 3.4 28.6 1.0
HZ3 E:LYS169 3.4 34.0 1.0
HZ2 E:LYS169 3.4 35.0 1.0
H3 E:CAP500 3.5 30.0 1.0
OE2 E:GLU195 3.6 42.8 1.0
ND2 F:ASN112 3.7 37.8 1.0
HD22 F:ASN112 3.7 37.9 1.0
N E:GLU195 3.7 29.6 1.0
NZ E:LYS169 3.8 34.6 1.0
HZ1 E:LYS169 3.8 34.8 1.0
OD2 E:ASP194 3.8 41.4 1.0
HB3 E:GLU195 3.8 36.3 1.0
NE2 E:HIS288 3.9 33.2 1.0
NZ E:LYS167 4.0 30.1 1.0
O7 E:CAP500 4.1 25.5 1.0
HZ1 E:LYS167 4.1 30.1 1.0
CA E:ASP194 4.1 27.8 1.0
CB E:ASP194 4.2 27.6 1.0
CG E:GLU195 4.2 37.0 1.0
HZ3 E:LYS167 4.2 30.0 1.0
NZ E:KCX192 4.2 32.8 1.0
HE1 E:HIS288 4.2 31.7 1.0
C1 E:CAP500 4.3 29.7 1.0
HD3 E:PRO196 4.3 36.2 1.0
HG12 E:ILE165 4.3 21.6 1.0
CB E:GLU195 4.4 35.2 1.0
C4 E:CAP500 4.4 30.6 1.0
CG2 E:ILE165 4.4 25.1 1.0
CE1 E:HIS288 4.4 32.1 1.0
C E:ASP194 4.4 29.3 1.0
H4 E:CAP500 4.6 30.1 1.0
H12 E:CAP500 4.6 28.2 1.0
CA E:GLU195 4.7 32.1 1.0
O1 E:CAP500 4.7 26.8 1.0
H52 E:CAP500 4.7 32.8 1.0
O F:HOH677 4.7 32.5 1.0
HG22 E:ILE165 4.7 24.2 1.0
HG3 E:LYS169 4.8 41.0 1.0
HG3 E:GLU195 4.8 37.3 1.0
HB3 E:ASP194 4.8 26.8 1.0
HG23 E:ILE165 4.9 23.4 1.0
CG F:ASN112 4.9 36.7 1.0
H11 E:CAP500 4.9 30.6 1.0
CD2 E:HIS288 4.9 33.0 1.0
HD13 E:ILE165 4.9 17.1 1.0
H51 E:CAP500 4.9 29.5 1.0
HG2 E:GLU195 4.9 35.8 1.0
HB2 E:ASP194 4.9 30.4 1.0
C5 E:CAP500 5.0 31.1 1.0

Magnesium binding site 6 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 6 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg501

b:32.1
occ:1.00
HO3 F:CAP500 1.5 40.7 1.0
OD1 F:ASP194 2.0 37.5 1.0
OE1 F:GLU195 2.0 30.7 1.0
OQ2 F:KCX192 2.0 25.8 1.0
O2 F:CAP500 2.1 36.4 1.0
O6 F:CAP500 2.1 27.0 1.0
O3 F:CAP500 2.3 39.5 1.0
HO2 F:CAP500 2.7 35.5 1.0
C2 F:CAP500 2.7 34.0 1.0
C F:CAP500 2.8 34.1 1.0
H F:GLU195 2.8 33.5 1.0
HD21 E:ASN112 2.9 32.2 1.0
C3 F:CAP500 3.0 33.9 1.0
CX F:KCX192 3.1 29.8 1.0
HZ2 F:LYS167 3.1 26.1 1.0
CD F:GLU195 3.1 33.7 1.0
CG F:ASP194 3.1 34.1 1.0
HG21 F:ILE165 3.3 28.5 1.0
OQ1 F:KCX192 3.3 33.6 1.0
HE2 F:HIS288 3.4 31.6 1.0
H3 F:CAP500 3.4 33.2 1.0
HZ3 F:LYS169 3.4 39.4 1.0
HZ2 F:LYS169 3.5 35.5 1.0
HA F:ASP194 3.5 26.1 1.0
ND2 E:ASN112 3.7 30.8 1.0
HD22 E:ASN112 3.7 30.5 1.0
OE2 F:GLU195 3.7 33.9 1.0
HZ1 F:LYS169 3.7 39.2 1.0
NZ F:LYS169 3.7 37.8 1.0
OD2 F:ASP194 3.8 38.8 1.0
N F:GLU195 3.8 32.6 1.0
NZ F:LYS167 3.9 28.4 1.0
HB3 F:GLU195 3.9 37.0 1.0
NE2 F:HIS288 4.0 31.8 1.0
O7 F:CAP500 4.0 36.3 1.0
HZ1 F:LYS167 4.0 30.2 1.0
HZ3 F:LYS167 4.1 28.9 1.0
C1 F:CAP500 4.2 33.0 1.0
CA F:ASP194 4.2 25.9 1.0
CB F:ASP194 4.2 27.6 1.0
HE1 F:HIS288 4.3 32.8 1.0
NZ F:KCX192 4.3 32.1 1.0
HG12 F:ILE165 4.3 31.9 1.0
CG F:GLU195 4.3 33.1 1.0
C4 F:CAP500 4.3 41.0 1.0
CG2 F:ILE165 4.4 27.9 1.0
HD3 F:PRO196 4.4 35.1 1.0
CE1 F:HIS288 4.4 32.3 1.0
CB F:GLU195 4.5 36.0 1.0
C F:ASP194 4.5 31.1 1.0
H4 F:CAP500 4.5 41.8 1.0
H11 F:CAP500 4.6 32.3 1.0
O1 F:CAP500 4.6 30.2 1.0
H52 F:CAP500 4.7 43.0 1.0
HG22 F:ILE165 4.7 27.1 1.0
CA F:GLU195 4.8 33.9 1.0
H12 F:CAP500 4.8 33.4 1.0
HG3 F:LYS169 4.8 39.8 1.0
HB3 F:ASP194 4.8 29.0 1.0
HG23 F:ILE165 4.9 27.5 1.0
HG3 F:GLU195 4.9 34.3 1.0
HD13 F:ILE165 4.9 24.8 1.0
O F:HOH728 4.9 39.4 1.0
CG E:ASN112 4.9 38.2 1.0
H51 F:CAP500 4.9 41.6 1.0
C5 F:CAP500 4.9 41.4 1.0
CD2 F:HIS288 5.0 33.5 1.0
O E:HOH725 5.0 35.0 1.0
HB2 F:ASP194 5.0 28.7 1.0

Magnesium binding site 7 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 7 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg501

b:33.2
occ:1.00
HO3 G:CAP500 1.4 36.7 1.0
OE1 G:GLU195 1.9 29.0 1.0
OQ2 G:KCX192 2.0 34.0 1.0
OD1 G:ASP194 2.0 33.0 1.0
O2 G:CAP500 2.2 36.2 1.0
O6 G:CAP500 2.2 35.1 1.0
O3 G:CAP500 2.2 37.0 1.0
HO2 G:CAP500 2.7 36.3 1.0
C2 G:CAP500 2.8 37.3 1.0
H G:GLU195 2.8 36.7 1.0
C G:CAP500 2.8 38.7 1.0
HD22 H:ASN112 3.0 40.2 1.0
C3 G:CAP500 3.0 36.8 1.0
CX G:KCX192 3.1 35.7 1.0
CD G:GLU195 3.1 45.8 1.0
HZ2 G:LYS167 3.2 40.7 1.0
CG G:ASP194 3.2 37.3 1.0
OQ1 G:KCX192 3.3 34.0 1.0
HE2 G:HIS288 3.3 34.0 1.0
H3 G:CAP500 3.4 34.7 1.0
HG21 G:ILE165 3.4 31.9 1.0
HZ2 G:LYS169 3.5 48.7 1.0
HZ3 G:LYS169 3.5 49.9 1.0
HA G:ASP194 3.5 37.8 1.0
HD21 H:ASN112 3.7 40.9 1.0
ND2 H:ASN112 3.7 39.9 1.0
OE2 G:GLU195 3.7 42.7 1.0
HZ1 G:LYS169 3.8 50.3 1.0
NZ G:LYS169 3.8 49.8 1.0
N G:GLU195 3.8 36.8 1.0
HB3 G:GLU195 3.9 38.3 1.0
OD2 G:ASP194 3.9 37.4 1.0
NE2 G:HIS288 3.9 34.2 1.0
NZ G:LYS167 4.0 40.9 1.0
O7 G:CAP500 4.0 40.3 1.0
HZ1 G:LYS167 4.1 41.9 1.0
HE1 G:HIS288 4.2 34.8 1.0
C1 G:CAP500 4.2 37.3 1.0
HZ3 G:LYS167 4.2 40.9 1.0
CA G:ASP194 4.2 34.9 1.0
CG G:GLU195 4.2 42.6 1.0
NZ G:KCX192 4.3 34.8 1.0
C4 G:CAP500 4.3 39.8 1.0
CB G:ASP194 4.3 34.8 1.0
HG12 G:ILE165 4.3 28.3 1.0
CE1 G:HIS288 4.4 33.6 1.0
HD3 G:PRO196 4.4 38.0 1.0
CB G:GLU195 4.4 37.7 1.0
CG2 G:ILE165 4.4 33.1 1.0
H4 G:CAP500 4.5 39.3 1.0
C G:ASP194 4.5 40.4 1.0
H12 G:CAP500 4.6 38.3 1.0
H52 G:CAP500 4.6 39.7 1.0
O1 G:CAP500 4.6 32.3 1.0
CA G:GLU195 4.7 36.8 1.0
HG22 G:ILE165 4.8 34.6 1.0
HG3 G:GLU195 4.8 42.9 1.0
H11 G:CAP500 4.8 37.3 1.0
H51 G:CAP500 4.8 39.4 1.0
C5 G:CAP500 4.8 39.7 1.0
CG H:ASN112 4.8 37.9 1.0
HG3 G:LYS169 4.9 32.5 1.0
O H:HOH715 4.9 42.4 1.0
CD2 G:HIS288 4.9 35.2 1.0
HB3 G:ASP194 4.9 35.5 1.0
HD13 G:ILE165 4.9 39.5 1.0
HG23 G:ILE165 4.9 30.8 1.0
HG2 G:GLU195 5.0 44.0 1.0

Magnesium binding site 8 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 8 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg501

b:33.0
occ:1.00
HO3 H:CAP500 1.5 36.5 1.0
OE1 H:GLU195 1.9 36.0 1.0
OQ2 H:KCX192 1.9 28.2 1.0
OD1 H:ASP194 1.9 33.1 1.0
O2 H:CAP500 2.2 39.4 1.0
O6 H:CAP500 2.2 31.0 1.0
O3 H:CAP500 2.3 36.2 1.0
H H:GLU195 2.7 31.6 1.0
HO2 H:CAP500 2.7 41.0 1.0
C2 H:CAP500 2.9 34.6 1.0
C H:CAP500 2.9 31.1 1.0
HD21 G:ASN112 3.0 41.7 1.0
CX H:KCX192 3.0 31.0 1.0
CD H:GLU195 3.0 46.4 1.0
C3 H:CAP500 3.1 32.8 1.0
CG H:ASP194 3.1 34.9 1.0
HZ2 H:LYS167 3.2 36.1 1.0
OQ1 H:KCX192 3.3 33.9 1.0
HG21 H:ILE165 3.4 30.5 1.0
HA H:ASP194 3.4 33.2 1.0
HZ3 H:LYS169 3.5 42.0 1.0
H3 H:CAP500 3.5 33.3 1.0
HZ2 H:LYS169 3.5 41.5 1.0
OE2 H:GLU195 3.6 38.1 1.0
N H:GLU195 3.7 32.0 1.0
ND2 G:ASN112 3.7 42.1 1.0
HD22 G:ASN112 3.7 42.6 1.0
NZ H:LYS169 3.8 41.8 1.0
HZ1 H:LYS169 3.8 42.4 1.0
OD2 H:ASP194 3.8 40.8 1.0
HB3 H:GLU195 3.8 34.4 1.0
NE2 H:HIS288 3.9 39.0 1.0
NZ H:LYS167 4.0 37.1 1.0
O7 H:CAP500 4.1 28.3 1.0
HZ1 H:LYS167 4.1 37.9 1.0
CA H:ASP194 4.1 31.3 1.0
HG12 H:ILE165 4.1 31.2 1.0
NZ H:KCX192 4.2 31.9 1.0
CB H:ASP194 4.2 32.9 1.0
CG H:GLU195 4.2 32.9 1.0
HE1 H:HIS288 4.2 38.1 1.0
HZ3 H:LYS167 4.3 38.2 1.0
C1 H:CAP500 4.3 34.7 1.0
HD3 H:PRO196 4.3 34.9 1.0
CB H:GLU195 4.4 34.7 1.0
C H:ASP194 4.4 33.8 1.0
C4 H:CAP500 4.4 33.1 1.0
CE1 H:HIS288 4.4 37.5 1.0
CG2 H:ILE165 4.5 30.9 1.0
H4 H:CAP500 4.6 32.0 1.0
H12 H:CAP500 4.6 34.2 1.0
CA H:GLU195 4.6 33.3 1.0
O1 H:CAP500 4.7 36.2 1.0
H52 H:CAP500 4.7 31.9 1.0
HG3 H:LYS169 4.8 47.6 1.0
HB3 H:ASP194 4.8 33.5 1.0
HG3 H:GLU195 4.8 32.3 1.0
HG23 H:ILE165 4.9 28.9 1.0
HG22 H:ILE165 4.9 31.0 1.0
H11 H:CAP500 4.9 35.8 1.0
CD2 H:HIS288 4.9 39.3 1.0
HB2 H:ASP194 4.9 32.9 1.0
HG2 H:GLU195 4.9 33.9 1.0
H51 H:CAP500 5.0 32.1 1.0
CG G:ASN112 5.0 37.8 1.0
C5 H:CAP500 5.0 31.5 1.0
O G:HOH718 5.0 42.7 1.0

Magnesium binding site 9 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 9 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg501

b:42.3
occ:1.00
HO3 I:CAP500 1.4 42.1 1.0
OE1 I:GLU195 1.9 31.0 1.0
OQ2 I:KCX192 2.0 38.6 1.0
OD1 I:ASP194 2.0 37.7 1.0
O2 I:CAP500 2.2 41.7 1.0
O3 I:CAP500 2.2 42.2 1.0
O6 I:CAP500 2.2 34.4 1.0
HO2 I:CAP500 2.7 41.0 1.0
H I:GLU195 2.8 29.2 1.0
C2 I:CAP500 2.8 41.1 1.0
C I:CAP500 2.8 40.6 1.0
HD21 J:ASN112 2.9 31.9 1.0
C3 I:CAP500 3.0 39.9 1.0
CX I:KCX192 3.1 35.6 1.0
CD I:GLU195 3.1 48.4 1.0
HZ2 I:LYS167 3.2 37.7 1.0
CG I:ASP194 3.2 37.6 1.0
OQ1 I:KCX192 3.3 33.7 1.0
HE2 I:HIS288 3.3 41.5 1.0
H3 I:CAP500 3.4 39.4 1.0
HG21 I:ILE165 3.4 37.4 1.0
HZ2 I:LYS169 3.5 34.1 1.0
HZ3 I:LYS169 3.5 34.5 1.0
HA I:ASP194 3.5 35.9 1.0
ND2 J:ASN112 3.6 30.4 1.0
OE2 I:GLU195 3.7 45.4 1.0
HD22 J:ASN112 3.7 28.7 1.0
N I:GLU195 3.8 31.2 1.0
HZ1 I:LYS169 3.8 36.0 1.0
NZ I:LYS169 3.8 35.2 1.0
HB3 I:GLU195 3.8 33.4 1.0
NE2 I:HIS288 3.9 39.8 1.0
OD2 I:ASP194 3.9 42.4 1.0
NZ I:LYS167 4.0 38.9 1.0
O7 I:CAP500 4.0 42.3 1.0
HE1 I:HIS288 4.1 38.9 1.0
HZ1 I:LYS167 4.2 39.4 1.0
CG I:GLU195 4.2 41.7 1.0
C1 I:CAP500 4.2 42.5 1.0
NZ I:KCX192 4.2 36.2 1.0
HZ3 I:LYS167 4.2 40.0 1.0
CA I:ASP194 4.2 34.2 1.0
C4 I:CAP500 4.3 40.8 1.0
CB I:ASP194 4.3 35.6 1.0
CE1 I:HIS288 4.3 39.0 1.0
HG12 I:ILE165 4.3 37.4 1.0
HD3 I:PRO196 4.4 37.6 1.0
CB I:GLU195 4.4 32.3 1.0
CG2 I:ILE165 4.5 36.6 1.0
C I:ASP194 4.5 34.8 1.0
H4 I:CAP500 4.5 41.3 1.0
H52 I:CAP500 4.6 41.1 1.0
H11 I:CAP500 4.6 41.5 1.0
O1 I:CAP500 4.7 41.4 1.0
CA I:GLU195 4.7 32.2 1.0
HG3 I:GLU195 4.8 40.1 1.0
HG22 I:ILE165 4.8 36.6 1.0
H12 I:CAP500 4.8 43.3 1.0
CG J:ASN112 4.8 37.1 1.0
H51 I:CAP500 4.8 40.1 1.0
C5 I:CAP500 4.9 40.2 1.0
CD2 I:HIS288 4.9 39.4 1.0
HG3 I:LYS169 4.9 38.2 1.0
HB3 I:ASP194 4.9 35.8 1.0
HG23 I:ILE165 4.9 35.1 1.0
HD13 I:ILE165 4.9 29.6 1.0
HG2 I:GLU195 5.0 41.1 1.0
O J:HOH612 5.0 48.2 1.0

Magnesium binding site 10 out of 12 in 5han

Go back to Magnesium Binding Sites List in 5han
Magnesium binding site 10 out of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg501

b:35.0
occ:1.00
HO3 J:CAP500 1.4 42.3 1.0
OE1 J:GLU195 1.9 39.6 1.0
OQ2 J:KCX192 2.0 31.1 1.0
OD1 J:ASP194 2.0 46.7 1.0
O2 J:CAP500 2.2 43.2 1.0
O6 J:CAP500 2.2 42.4 1.0
O3 J:CAP500 2.2 43.5 1.0
HO2 J:CAP500 2.7 42.6 1.0
H J:GLU195 2.8 32.2 1.0
C2 J:CAP500 2.8 43.5 1.0
C J:CAP500 2.8 41.4 1.0
HD21 I:ASN112 2.9 40.6 1.0
C3 J:CAP500 3.0 44.6 1.0
CX J:KCX192 3.0 34.0 1.0
CD J:GLU195 3.1 44.8 1.0
HZ2 J:LYS167 3.2 33.0 1.0
CG J:ASP194 3.2 42.4 1.0
OQ1 J:KCX192 3.3 37.9 1.0
HG21 J:ILE165 3.4 30.8 1.0
H3 J:CAP500 3.4 45.2 1.0
HZ2 J:LYS169 3.5 44.0 1.0
HZ3 J:LYS169 3.5 45.1 1.0
HA J:ASP194 3.5 23.5 1.0
OE2 J:GLU195 3.6 40.6 1.0
ND2 I:ASN112 3.7 40.7 1.0
HD22 I:ASN112 3.7 40.3 1.0
N J:GLU195 3.8 31.6 1.0
NZ J:LYS169 3.8 45.3 1.0
HZ1 J:LYS169 3.8 46.1 1.0
HB3 J:GLU195 3.8 31.5 1.0
OD2 J:ASP194 3.8 47.8 1.0
NE2 J:HIS288 3.9 37.5 1.0
NZ J:LYS167 4.0 31.9 1.0
O7 J:CAP500 4.1 45.0 1.0
HZ1 J:LYS167 4.1 32.1 1.0
HE1 J:HIS288 4.2 37.1 1.0
CA J:ASP194 4.2 28.6 1.0
NZ J:KCX192 4.2 32.1 1.0
CG J:GLU195 4.2 44.3 1.0
HZ3 J:LYS167 4.2 31.2 1.0
C1 J:CAP500 4.3 44.2 1.0
CB J:ASP194 4.3 30.2 1.0
HG12 J:ILE165 4.3 34.7 1.0
HD3 J:PRO196 4.3 37.4 1.0
C4 J:CAP500 4.4 43.4 1.0
CE1 J:HIS288 4.4 36.3 1.0
CB J:GLU195 4.4 31.7 1.0
CG2 J:ILE165 4.4 30.9 1.0
C J:ASP194 4.5 35.2 1.0
H4 J:CAP500 4.6 42.8 1.0
H12 J:CAP500 4.6 44.1 1.0
H52 J:CAP500 4.6 38.7 1.0
O1 J:CAP500 4.7 41.6 1.0
CA J:GLU195 4.7 30.7 1.0
HG22 J:ILE165 4.8 31.4 1.0
HG3 J:GLU195 4.8 44.7 1.0
HG3 J:LYS169 4.8 32.8 1.0
HB3 J:ASP194 4.9 31.4 1.0
H11 J:CAP500 4.9 44.8 1.0
CD2 J:HIS288 4.9 37.4 1.0
H51 J:CAP500 4.9 39.5 1.0
HG23 J:ILE165 4.9 29.2 1.0
CG I:ASN112 4.9 45.5 1.0
C5 J:CAP500 4.9 39.8 1.0
HD13 J:ILE165 4.9 35.3 1.0
HG2 J:GLU195 5.0 43.3 1.0

Reference:

M.A.Arbing, S.Satagopan, V.A.Varaljay, J.G.Leong, F.R.Tabita. Structure Function Studies of R. Palustris Rubisco To Be Published.
Page generated: Mon Dec 14 20:26:41 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy