Atomistry » Magnesium » PDB 5kfu-5ktd » 5koz
Atomistry »
  Magnesium »
    PDB 5kfu-5ktd »
      5koz »

Magnesium in PDB 5koz: Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)

Enzymatic activity of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound)

All present enzymatic activity of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound):
4.1.1.39;

Protein crystallography data

The structure of Structure Function Studies of R. Palustris Rubisco (K192C Mutant; Cabp-Bound), PDB code: 5koz was solved by M.A.Arbing, J.A.North, S.Satagopan, F.R.Tabita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 11.50 / 2.30
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 75.460, 110.620, 166.850, 89.96, 101.77, 104.88
R / Rfree (%) 20 / 24.7

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 (K192C Mutant; Cabp-Bound) (pdb code 5koz). 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 (K192C Mutant; Cabp-Bound), PDB code: 5koz:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 1 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:44.6
occ:1.00
OD1 A:ASP194 1.9 42.3 1.0
HO2 A:CAP500 2.0 50.9 1.0
O2 A:CAP500 2.0 42.4 1.0
O7 A:CAP500 2.1 41.5 1.0
OE1 A:GLU195 2.2 47.0 1.0
O2 A:CO3502 2.2 54.2 1.0
O3 A:CAP500 2.4 38.4 1.0
C2 A:CAP500 2.7 43.1 1.0
C A:CAP500 2.7 42.3 1.0
HZ3 A:LYS169 2.9 55.6 1.0
CG A:ASP194 3.0 43.1 1.0
HD21 B:ASN112 3.0 64.6 1.0
HO3 A:CAP500 3.1 46.1 1.0
CD A:GLU195 3.1 49.6 1.0
HZ3 A:LYS167 3.1 48.8 1.0
C3 A:CAP500 3.1 41.4 1.0
HZ1 A:LYS169 3.2 55.6 1.0
H A:GLU195 3.2 53.2 1.0
HZ1 A:LYS167 3.2 48.8 1.0
NZ A:LYS169 3.3 46.3 1.0
HZ2 A:LYS169 3.4 55.6 1.0
C A:CO3502 3.4 54.4 1.0
OE2 A:GLU195 3.4 49.7 1.0
OD2 A:ASP194 3.5 44.1 1.0
HG21 A:ILE165 3.5 45.9 1.0
NZ A:LYS167 3.5 40.6 1.0
HA A:ASP194 3.6 49.6 1.0
HD22 B:ASN112 3.7 64.6 1.0
ND2 B:ASN112 3.7 53.9 1.0
H3 A:CAP500 3.7 49.6 1.0
HZ2 A:LYS167 3.8 48.8 1.0
O1 A:CO3502 3.8 53.7 1.0
O6 A:CAP500 4.0 42.4 1.0
N A:GLU195 4.0 44.4 1.0
C1 A:CAP500 4.1 44.0 1.0
CB A:ASP194 4.2 42.1 1.0
CA A:ASP194 4.3 41.4 1.0
HB3 A:GLU195 4.3 57.8 1.0
NE2 A:HIS288 4.3 48.8 1.0
HG12 A:ILE165 4.3 46.5 1.0
HD3 A:PRO196 4.4 47.0 1.0
C4 A:CAP500 4.4 42.6 1.0
O1 A:CAP500 4.4 44.0 1.0
CG2 A:ILE165 4.5 38.2 1.0
H4 A:CAP500 4.5 51.1 1.0
CG A:GLU195 4.5 49.7 1.0
O3 A:CO3502 4.5 55.0 1.0
HG3 A:LYS169 4.5 53.6 1.0
O B:HOH705 4.6 36.6 1.0
H12 A:CAP500 4.6 52.8 1.0
C A:ASP194 4.7 42.8 1.0
O B:HOH603 4.7 26.7 1.0
HB3 A:ASP194 4.7 50.6 1.0
HE1 A:HIS288 4.7 58.5 1.0
CB A:GLU195 4.8 48.2 1.0
CE A:LYS169 4.8 46.4 1.0
HB2 A:ASP194 4.8 50.6 1.0
CE1 A:HIS288 4.8 48.7 1.0
H11 A:CAP500 4.9 52.8 1.0
HG22 A:ILE165 4.9 45.9 1.0
HG23 A:ILE165 4.9 45.9 1.0
CE A:LYS167 4.9 42.1 1.0
CG B:ASN112 4.9 52.5 1.0
H51 A:CAP500 4.9 51.6 1.0
HE2 A:LYS167 4.9 50.5 1.0
HG3 A:GLU195 5.0 59.6 1.0

Magnesium binding site 2 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 2 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:44.5
occ:1.00
O1 B:CO3502 1.9 43.7 1.0
O3 B:CAP500 1.9 44.4 1.0
OE1 B:GLU195 1.9 43.4 1.0
HO2 B:CAP500 2.0 49.7 1.0
OD1 B:ASP194 2.2 47.1 1.0
O2 B:CAP500 2.3 41.4 1.0
O6 B:CAP500 2.3 46.1 1.0
HO3 B:CAP500 2.6 53.3 1.0
C2 B:CAP500 2.8 43.6 1.0
C3 B:CAP500 2.9 43.2 1.0
C B:CAP500 2.9 45.5 1.0
C B:CO3502 2.9 42.7 1.0
H B:GLU195 3.0 50.2 1.0
HD21 A:ASN112 3.0 48.4 1.0
CD B:GLU195 3.1 42.2 1.0
CG B:ASP194 3.3 47.3 1.0
O2 B:CO3502 3.4 41.9 1.0
HZ3 B:LYS169 3.4 51.0 1.0
H3 B:CAP500 3.4 51.8 1.0
HG21 B:ILE165 3.5 51.7 1.0
HZ2 B:LYS169 3.5 51.0 1.0
HZ1 B:LYS169 3.6 51.0 1.0
HA B:ASP194 3.6 52.4 1.0
OE2 B:GLU195 3.6 42.9 1.0
HZ1 B:LYS167 3.7 50.3 1.0
ND2 A:ASN112 3.7 40.4 1.0
HZ3 B:LYS167 3.7 50.3 1.0
NZ B:LYS169 3.7 42.5 1.0
HD22 A:ASN112 3.7 48.4 1.0
NE2 B:HIS288 3.8 40.6 1.0
HB3 B:GLU195 3.8 49.5 1.0
N B:GLU195 3.9 41.8 1.0
OD2 B:ASP194 4.0 48.6 1.0
O3 B:CO3502 4.0 43.4 1.0
O7 B:CAP500 4.1 46.8 1.0
NZ B:LYS167 4.1 41.9 1.0
C4 B:CAP500 4.1 42.6 1.0
H4 B:CAP500 4.2 51.1 1.0
HG12 B:ILE165 4.2 50.8 1.0
C1 B:CAP500 4.3 44.4 1.0
HE1 B:HIS288 4.3 49.1 1.0
CA B:ASP194 4.3 43.7 1.0
CG B:GLU195 4.3 41.2 1.0
CE1 B:HIS288 4.4 40.9 1.0
H51 B:CAP500 4.4 50.0 1.0
CB B:ASP194 4.4 45.6 1.0
CB B:GLU195 4.4 41.2 1.0
HZ2 B:LYS167 4.5 50.3 1.0
CG2 B:ILE165 4.5 43.1 1.0
HD3 B:PRO196 4.5 58.5 1.0
C B:ASP194 4.6 43.0 1.0
H11 B:CAP500 4.7 53.3 1.0
O1 B:CAP500 4.7 45.6 1.0
C5 B:CAP500 4.7 41.7 1.0
CD2 B:HIS288 4.8 39.9 1.0
CA B:GLU195 4.8 41.4 1.0
HG3 B:GLU195 4.8 49.5 1.0
HG23 B:ILE165 4.8 51.7 1.0
H52 B:CAP500 4.9 50.0 1.0
CG A:ASN112 4.9 40.5 1.0
H12 B:CAP500 4.9 53.3 1.0
HB3 B:ASP194 4.9 54.7 1.0
HG2 B:GLU195 4.9 49.5 1.0
HD2 B:HIS288 5.0 47.9 1.0
HG22 B:ILE165 5.0 51.7 1.0
HG3 B:LYS169 5.0 54.4 1.0

Magnesium binding site 3 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 3 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg501

b:36.0
occ:1.00
OD1 C:ASP194 1.9 34.0 1.0
OE1 C:GLU195 2.0 38.6 1.0
HO2 C:CAP500 2.1 33.9 1.0
O3 C:CO3502 2.2 34.9 1.0
O6 C:CAP500 2.2 31.8 1.0
O2 C:CAP500 2.2 28.3 1.0
O3 C:CAP500 2.4 29.8 1.0
C C:CAP500 2.9 31.0 1.0
C2 C:CAP500 2.9 29.1 1.0
H C:GLU195 2.9 44.8 1.0
HZ3 C:LYS169 3.0 42.6 1.0
HO3 C:CAP500 3.0 35.7 1.0
CG C:ASP194 3.1 35.1 1.0
HD21 D:ASN112 3.1 34.8 1.0
CD C:GLU195 3.1 40.8 1.0
C3 C:CAP500 3.2 28.9 1.0
HZ1 C:LYS169 3.2 42.6 1.0
HZ2 C:LYS169 3.2 42.6 1.0
C C:CO3502 3.3 38.4 1.0
HZ3 C:LYS167 3.3 35.5 1.0
NZ C:LYS169 3.3 35.5 1.0
HZ1 C:LYS167 3.4 35.5 1.0
HA C:ASP194 3.5 39.9 1.0
HG21 C:ILE165 3.5 42.1 1.0
OE2 C:GLU195 3.5 40.4 1.0
HE2 C:HIS288 3.6 44.5 1.0
O2 C:CO3502 3.6 38.6 1.0
HD22 D:ASN112 3.6 34.8 1.0
ND2 D:ASN112 3.7 29.0 1.0
OD2 C:ASP194 3.7 36.8 1.0
H3 C:CAP500 3.8 34.7 1.0
N C:GLU195 3.8 37.3 1.0
NZ C:LYS167 3.8 29.6 1.0
HB3 C:GLU195 3.9 49.9 1.0
O7 C:CAP500 4.1 31.6 1.0
HZ2 C:LYS167 4.2 35.5 1.0
NE2 C:HIS288 4.2 37.1 1.0
CA C:ASP194 4.2 33.2 1.0
CB C:ASP194 4.2 34.3 1.0
HG12 C:ILE165 4.2 42.3 1.0
C1 C:CAP500 4.3 28.7 1.0
CG C:GLU195 4.3 41.6 1.0
HD3 C:PRO196 4.3 47.5 1.0
O1 C:CO3502 4.4 40.0 1.0
CB C:GLU195 4.5 41.5 1.0
CG2 C:ILE165 4.5 35.1 1.0
C4 C:CAP500 4.5 28.7 1.0
C C:ASP194 4.5 35.1 1.0
HG3 C:LYS169 4.5 44.4 1.0
H4 C:CAP500 4.6 34.5 1.0
HE1 C:HIS288 4.6 44.2 1.0
O1 C:CAP500 4.6 29.6 1.0
HB3 C:ASP194 4.7 41.2 1.0
CE1 C:HIS288 4.7 36.8 1.0
CA C:GLU195 4.8 40.5 1.0
O C:HOH649 4.8 23.3 1.0
H12 C:CAP500 4.8 34.4 1.0
H51 C:CAP500 4.8 34.3 1.0
CE C:LYS169 4.8 36.1 1.0
O D:HOH652 4.8 41.1 1.0
HG23 C:ILE165 4.8 42.1 1.0
HB2 C:ASP194 4.9 41.2 1.0
HG2 C:GLU195 4.9 49.9 1.0
HG3 C:GLU195 4.9 49.9 1.0
CG D:ASN112 4.9 27.8 1.0
HG22 C:ILE165 4.9 42.1 1.0

Magnesium binding site 4 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 4 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg501

b:35.6
occ:1.00
OD1 D:ASP194 2.0 37.1 1.0
O3 D:CO3502 2.0 41.9 1.0
HO2 D:CAP500 2.0 42.6 1.0
O6 D:CAP500 2.1 32.1 1.0
O2 D:CAP500 2.1 35.5 1.0
OE1 D:GLU195 2.1 38.2 1.0
O3 D:CAP500 2.3 32.6 1.0
C2 D:CAP500 2.7 32.1 1.0
C D:CAP500 2.7 30.3 1.0
C D:CO3502 2.9 43.0 1.0
HO3 D:CAP500 2.9 39.2 1.0
H D:GLU195 3.1 41.6 1.0
C3 D:CAP500 3.1 31.7 1.0
CG D:ASP194 3.1 35.9 1.0
O2 D:CO3502 3.1 42.8 1.0
HD21 C:ASN112 3.2 39.8 1.0
CD D:GLU195 3.2 38.2 1.0
HZ3 D:LYS169 3.3 48.6 1.0
HG21 D:ILE165 3.3 49.3 1.0
HZ3 D:LYS167 3.3 45.0 1.0
HZ1 D:LYS167 3.4 45.0 1.0
HA D:ASP194 3.5 38.9 1.0
HZ1 D:LYS169 3.5 48.6 1.0
HE2 D:HIS288 3.5 42.3 1.0
HZ2 D:LYS169 3.6 48.6 1.0
NZ D:LYS169 3.6 40.5 1.0
H3 D:CAP500 3.7 38.1 1.0
OE2 D:GLU195 3.7 37.5 1.0
OD2 D:ASP194 3.7 37.4 1.0
ND2 C:ASN112 3.8 33.1 1.0
HD22 C:ASN112 3.8 39.8 1.0
NZ D:LYS167 3.8 37.5 1.0
N D:GLU195 3.9 34.7 1.0
O7 D:CAP500 4.0 29.6 1.0
HG12 D:ILE165 4.0 48.9 1.0
HB3 D:GLU195 4.0 45.6 1.0
O1 D:CO3502 4.1 43.8 1.0
NE2 D:HIS288 4.1 35.3 1.0
C1 D:CAP500 4.2 31.5 1.0
CA D:ASP194 4.2 32.4 1.0
HZ2 D:LYS167 4.2 45.0 1.0
CB D:ASP194 4.2 34.2 1.0
CG2 D:ILE165 4.3 41.1 1.0
C4 D:CAP500 4.3 31.1 1.0
H4 D:CAP500 4.3 37.3 1.0
CG D:GLU195 4.5 38.8 1.0
O1 D:CAP500 4.5 30.9 1.0
HE1 D:HIS288 4.6 42.2 1.0
HD3 D:PRO196 4.6 36.1 1.0
C D:ASP194 4.6 33.0 1.0
CB D:GLU195 4.6 38.0 1.0
H11 D:CAP500 4.6 37.9 1.0
HG23 D:ILE165 4.7 49.3 1.0
CE1 D:HIS288 4.7 35.1 1.0
HB3 D:ASP194 4.8 41.1 1.0
H51 D:CAP500 4.8 36.1 1.0
HG22 D:ILE165 4.8 49.3 1.0
HG3 D:LYS169 4.8 48.5 1.0
CG1 D:ILE165 4.8 40.7 1.0
HD13 D:ILE165 4.8 49.5 1.0
HB2 D:ASP194 4.9 41.1 1.0
H12 D:CAP500 4.9 37.9 1.0
CA D:GLU195 4.9 35.7 1.0
HE2 D:LYS167 5.0 46.0 1.0
O C:HOH621 5.0 35.0 1.0
HB D:ILE165 5.0 48.4 1.0

Magnesium binding site 5 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 5 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg501

b:45.2
occ:1.00
O1 E:CO3502 1.9 42.3 1.0
OE1 E:GLU195 2.0 42.9 1.0
OD1 E:ASP194 2.1 49.9 1.0
HO2 E:CAP500 2.2 53.4 1.0
O7 E:CAP500 2.2 43.7 1.0
O3 E:CAP500 2.3 41.9 1.0
O2 E:CAP500 2.4 44.5 1.0
HO3 E:CAP500 2.9 50.3 1.0
H E:GLU195 2.9 51.5 1.0
C E:CO3502 2.9 39.5 1.0
C E:CAP500 2.9 44.3 1.0
HD21 F:ASN112 3.0 50.8 1.0
C2 E:CAP500 3.0 43.9 1.0
CD E:GLU195 3.1 41.4 1.0
C3 E:CAP500 3.2 42.7 1.0
HE2 E:HIS288 3.2 44.0 1.0
CG E:ASP194 3.3 50.0 1.0
O2 E:CO3502 3.3 37.0 1.0
HZ3 E:LYS169 3.4 51.9 1.0
HG21 E:ILE165 3.4 54.5 1.0
HA E:ASP194 3.5 55.1 1.0
HZ2 E:LYS169 3.6 51.9 1.0
ND2 F:ASN112 3.6 42.3 1.0
OE2 E:GLU195 3.6 41.8 1.0
HZ1 E:LYS169 3.7 51.9 1.0
HB3 E:GLU195 3.7 50.3 1.0
HD22 F:ASN112 3.7 50.8 1.0
HZ3 E:LYS167 3.7 55.9 1.0
N E:GLU195 3.7 42.9 1.0
HZ1 E:LYS167 3.8 55.9 1.0
NZ E:LYS169 3.8 43.3 1.0
H3 E:CAP500 3.8 51.2 1.0
NE2 E:HIS288 3.8 36.6 1.0
OD2 E:ASP194 3.9 51.2 1.0
O3 E:CO3502 4.1 41.9 1.0
O6 E:CAP500 4.1 44.7 1.0
NZ E:LYS167 4.2 46.6 1.0
HG12 E:ILE165 4.2 53.0 1.0
CA E:ASP194 4.2 45.9 1.0
CG E:GLU195 4.3 42.2 1.0
CB E:GLU195 4.3 41.9 1.0
CB E:ASP194 4.3 48.9 1.0
HE1 E:HIS288 4.3 43.6 1.0
CG2 E:ILE165 4.4 45.4 1.0
H4 E:CAP500 4.4 51.2 1.0
CE1 E:HIS288 4.4 36.3 1.0
C4 E:CAP500 4.4 42.6 1.0
C1 E:CAP500 4.4 44.1 1.0
C E:ASP194 4.5 46.4 1.0
HD3 E:PRO196 4.5 45.8 1.0
HZ2 E:LYS167 4.6 55.9 1.0
CA E:GLU195 4.6 40.7 1.0
HG23 E:ILE165 4.7 54.5 1.0
H51 E:CAP500 4.7 49.0 1.0
CD2 E:HIS288 4.8 36.4 1.0
O1 E:CAP500 4.8 44.5 1.0
HG3 E:GLU195 4.8 50.7 1.0
CG F:ASN112 4.8 40.9 1.0
HG3 E:LYS169 4.8 50.6 1.0
HB3 E:ASP194 4.8 58.7 1.0
HG22 E:ILE165 4.9 54.5 1.0
HG2 E:GLU195 4.9 50.7 1.0
H12 E:CAP500 4.9 52.9 1.0
HB2 E:ASP194 5.0 58.7 1.0
HD2 E:HIS288 5.0 43.6 1.0

Magnesium binding site 6 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 6 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg501

b:38.4
occ:1.00
O3 F:CO3502 1.9 35.2 1.0
OD1 F:ASP194 2.0 41.1 1.0
OE1 F:GLU195 2.0 37.6 1.0
HO2 F:CAP500 2.2 47.1 1.0
O7 F:CAP500 2.3 38.3 1.0
O3 F:CAP500 2.3 35.6 1.0
O2 F:CAP500 2.4 39.3 1.0
H F:GLU195 2.8 48.3 1.0
HO3 F:CAP500 2.9 42.7 1.0
C F:CAP500 3.0 38.2 1.0
C2 F:CAP500 3.0 37.8 1.0
C F:CO3502 3.0 36.8 1.0
CD F:GLU195 3.1 39.9 1.0
CG F:ASP194 3.2 43.6 1.0
HD21 E:ASN112 3.2 41.2 1.0
C3 F:CAP500 3.2 36.5 1.0
HG21 F:ILE165 3.3 40.2 1.0
HZ3 F:LYS169 3.3 44.1 1.0
O1 F:CO3502 3.4 35.7 1.0
HA F:ASP194 3.4 51.3 1.0
HZ3 F:LYS167 3.5 53.7 1.0
HZ1 F:LYS167 3.6 53.7 1.0
N F:GLU195 3.7 40.3 1.0
HZ2 F:LYS169 3.7 44.1 1.0
HZ1 F:LYS169 3.7 44.1 1.0
HB3 F:GLU195 3.7 48.2 1.0
OE2 F:GLU195 3.7 39.7 1.0
H3 F:CAP500 3.8 43.8 1.0
NZ F:LYS169 3.8 36.7 1.0
ND2 E:ASN112 3.9 34.3 1.0
HD22 E:ASN112 3.9 41.2 1.0
OD2 F:ASP194 3.9 44.7 1.0
NZ F:LYS167 4.0 44.8 1.0
NE2 F:HIS288 4.0 37.1 1.0
HG12 F:ILE165 4.1 41.5 1.0
CA F:ASP194 4.1 42.8 1.0
O2 F:CO3502 4.2 39.3 1.0
O6 F:CAP500 4.2 37.8 1.0
CB F:ASP194 4.2 43.4 1.0
CG2 F:ILE165 4.3 33.5 1.0
CG F:GLU195 4.3 40.7 1.0
CB F:GLU195 4.3 40.1 1.0
HZ2 F:LYS167 4.3 53.7 1.0
HD3 F:PRO196 4.4 40.9 1.0
HE1 F:HIS288 4.4 45.2 1.0
C1 F:CAP500 4.4 37.3 1.0
C F:ASP194 4.4 41.4 1.0
C4 F:CAP500 4.5 38.0 1.0
CE1 F:HIS288 4.5 37.7 1.0
H4 F:CAP500 4.6 45.6 1.0
HG23 F:ILE165 4.6 40.2 1.0
CA F:GLU195 4.6 39.4 1.0
HB3 F:ASP194 4.7 52.1 1.0
HG22 F:ILE165 4.8 40.2 1.0
HG3 F:LYS169 4.8 45.1 1.0
O1 F:CAP500 4.8 37.0 1.0
H51 F:CAP500 4.8 44.8 1.0
HG3 F:GLU195 4.9 48.9 1.0
H11 F:CAP500 4.9 44.8 1.0
HG2 F:GLU195 4.9 48.9 1.0
CD2 F:HIS288 4.9 37.4 1.0
CG1 F:ILE165 4.9 34.6 1.0
HB2 F:ASP194 4.9 52.1 1.0

Magnesium binding site 7 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 7 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg501

b:32.6
occ:1.00
HO2 G:CAP500 1.9 42.4 1.0
O2 G:CO3502 2.0 35.0 1.0
OD1 G:ASP194 2.0 33.8 1.0
O2 G:CAP500 2.1 35.3 1.0
O3 G:CAP500 2.1 33.6 1.0
OE1 G:GLU195 2.1 35.2 1.0
O7 G:CAP500 2.3 33.6 1.0
C2 G:CAP500 2.7 34.3 1.0
HO3 G:CAP500 2.8 40.3 1.0
C G:CAP500 2.8 34.4 1.0
C3 G:CAP500 3.0 32.8 1.0
C G:CO3502 3.0 34.5 1.0
HD21 H:ASN112 3.0 39.3 1.0
H G:GLU195 3.1 37.5 1.0
CG G:ASP194 3.2 32.3 1.0
O1 G:CO3502 3.2 32.2 1.0
CD G:GLU195 3.2 36.0 1.0
HZ3 G:LYS169 3.3 50.5 1.0
HG21 G:ILE165 3.4 37.2 1.0
HZ3 G:LYS167 3.4 39.1 1.0
HZ1 G:LYS169 3.5 50.5 1.0
H3 G:CAP500 3.5 39.4 1.0
HZ1 G:LYS167 3.5 39.1 1.0
HZ2 G:LYS169 3.5 50.5 1.0
HA G:ASP194 3.6 37.8 1.0
NZ G:LYS169 3.6 42.1 1.0
ND2 H:ASN112 3.7 32.8 1.0
OE2 G:GLU195 3.7 35.5 1.0
HD22 H:ASN112 3.7 39.3 1.0
OD2 G:ASP194 3.8 33.4 1.0
NZ G:LYS167 3.9 32.6 1.0
N G:GLU195 3.9 31.2 1.0
HB3 G:GLU195 4.0 42.1 1.0
NE2 G:HIS288 4.1 30.7 1.0
HG12 G:ILE165 4.1 39.1 1.0
O6 G:CAP500 4.1 35.0 1.0
C1 G:CAP500 4.2 34.5 1.0
O3 G:CO3502 4.2 36.9 1.0
HZ2 G:LYS167 4.2 39.1 1.0
C4 G:CAP500 4.2 33.9 1.0
CA G:ASP194 4.3 31.4 1.0
CB G:ASP194 4.3 31.9 1.0
H4 G:CAP500 4.3 40.6 1.0
CG2 G:ILE165 4.4 31.0 1.0
CG G:GLU195 4.5 36.2 1.0
O1 G:CAP500 4.6 35.0 1.0
HD3 G:PRO196 4.6 36.4 1.0
H12 G:CAP500 4.6 41.4 1.0
HE1 G:HIS288 4.6 36.5 1.0
CB G:GLU195 4.6 35.1 1.0
H52 G:CAP500 4.6 40.6 1.0
C G:ASP194 4.6 31.1 1.0
CE1 G:HIS288 4.7 30.4 1.0
HG23 G:ILE165 4.8 37.2 1.0
HB3 G:ASP194 4.8 38.3 1.0
HG3 G:LYS169 4.8 49.7 1.0
H11 G:CAP500 4.9 41.4 1.0
HG22 G:ILE165 4.9 37.2 1.0
CA G:GLU195 4.9 33.0 1.0
CG H:ASN112 4.9 33.8 1.0
CG1 G:ILE165 4.9 32.6 1.0
C5 G:CAP500 4.9 33.8 1.0
O H:HOH701 4.9 29.0 1.0
HB2 G:ASP194 4.9 38.3 1.0
HD13 G:ILE165 5.0 41.6 1.0
CD2 G:HIS288 5.0 30.4 1.0

Magnesium binding site 8 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 8 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg501

b:43.6
occ:1.00
OD1 H:ASP194 2.0 39.5 1.0
O1 H:CO3502 2.0 53.2 1.0
HO2 H:CAP500 2.0 49.3 1.0
OE1 H:GLU195 2.1 38.0 1.0
O2 H:CAP500 2.2 41.0 1.0
O6 H:CAP500 2.2 38.3 1.0
O3 H:CAP500 2.2 39.6 1.0
C2 H:CAP500 2.8 40.1 1.0
C H:CAP500 2.8 39.4 1.0
HO3 H:CAP500 2.9 47.6 1.0
H H:GLU195 2.9 37.6 1.0
C3 H:CAP500 3.1 39.5 1.0
C H:CO3502 3.1 62.3 1.0
CG H:ASP194 3.1 38.0 1.0
HD21 G:ASN112 3.2 40.0 1.0
CD H:GLU195 3.2 36.0 1.0
HG21 H:ILE165 3.3 40.6 1.0
HA H:ASP194 3.3 40.2 1.0
HZ3 H:LYS169 3.4 37.0 1.0
O3 H:CO3502 3.4 64.6 1.0
HZ1 H:LYS169 3.5 37.0 1.0
HZ3 H:LYS167 3.5 37.5 1.0
HZ2 H:LYS169 3.5 37.0 1.0
H3 H:CAP500 3.6 47.4 1.0
NZ H:LYS169 3.7 30.9 1.0
OD2 H:ASP194 3.7 39.1 1.0
N H:GLU195 3.7 31.4 1.0
HZ1 H:LYS167 3.7 37.5 1.0
OE2 H:GLU195 3.8 36.0 1.0
ND2 G:ASN112 3.8 33.4 1.0
HD22 G:ASN112 3.8 40.0 1.0
HB3 H:GLU195 3.9 38.7 1.0
NE2 H:HIS288 4.0 38.0 1.0
HG12 H:ILE165 4.1 40.6 1.0
CA H:ASP194 4.1 33.5 1.0
O7 H:CAP500 4.1 39.6 1.0
NZ H:LYS167 4.1 31.2 1.0
CB H:ASP194 4.2 35.2 1.0
O2 H:CO3502 4.2 65.2 1.0
C1 H:CAP500 4.2 40.9 1.0
CG2 H:ILE165 4.3 33.8 1.0
C4 H:CAP500 4.3 39.1 1.0
H4 H:CAP500 4.4 47.0 1.0
CG H:GLU195 4.4 34.1 1.0
C H:ASP194 4.4 33.5 1.0
HE1 H:HIS288 4.5 45.5 1.0
CB H:GLU195 4.5 32.3 1.0
HZ2 H:LYS167 4.5 37.5 1.0
HD3 H:PRO196 4.5 40.4 1.0
CE1 H:HIS288 4.6 37.9 1.0
O1 H:CAP500 4.7 41.0 1.0
HG23 H:ILE165 4.7 40.6 1.0
H11 H:CAP500 4.7 49.1 1.0
H52 H:CAP500 4.7 45.1 1.0
HB3 H:ASP194 4.7 42.2 1.0
CA H:GLU195 4.7 31.1 1.0
HG22 H:ILE165 4.8 40.6 1.0
HB2 H:ASP194 4.8 42.2 1.0
CG1 H:ILE165 4.9 33.9 1.0
HG3 H:LYS169 4.9 38.4 1.0
H12 H:CAP500 4.9 49.1 1.0
HD13 H:ILE165 5.0 41.6 1.0
CD2 H:HIS288 5.0 37.5 1.0
C5 H:CAP500 5.0 37.6 1.0
HB H:ILE165 5.0 41.1 1.0
HG3 H:GLU195 5.0 40.9 1.0

Magnesium binding site 9 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 9 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg501

b:39.5
occ:1.00
O2 I:CO3502 1.9 40.0 1.0
OE1 I:GLU195 1.9 41.5 1.0
OD1 I:ASP194 2.0 35.0 1.0
O6 I:CAP500 2.1 37.1 1.0
HO2 I:CAP500 2.3 44.8 1.0
O3 I:CAP500 2.3 32.8 1.0
O2 I:CAP500 2.4 37.3 1.0
C I:CAP500 2.8 38.0 1.0
HO3 I:CAP500 2.9 39.3 1.0
H I:GLU195 2.9 46.1 1.0
C2 I:CAP500 2.9 36.4 1.0
CD I:GLU195 3.0 44.2 1.0
C I:CO3502 3.0 45.0 1.0
HD21 J:ASN112 3.1 39.5 1.0
C3 I:CAP500 3.2 34.0 1.0
CG I:ASP194 3.2 35.6 1.0
HZ3 I:LYS169 3.2 48.4 1.0
HZ2 I:LYS169 3.3 48.4 1.0
HE2 I:HIS288 3.3 51.0 1.0
HZ1 I:LYS169 3.4 48.4 1.0
OE2 I:GLU195 3.5 44.4 1.0
O3 I:CO3502 3.5 46.1 1.0
HA I:ASP194 3.5 41.9 1.0
NZ I:LYS169 3.5 40.3 1.0
HG21 I:ILE165 3.5 46.8 1.0
HZ3 I:LYS167 3.6 42.1 1.0
HD22 J:ASN112 3.7 39.5 1.0
HZ1 I:LYS167 3.7 42.1 1.0
ND2 J:ASN112 3.7 32.9 1.0
N I:GLU195 3.7 38.4 1.0
H3 I:CAP500 3.7 40.8 1.0
HB3 I:GLU195 3.8 52.0 1.0
OD2 I:ASP194 3.9 36.8 1.0
NE2 I:HIS288 3.9 42.5 1.0
O7 I:CAP500 4.0 38.8 1.0
NZ I:LYS167 4.1 35.1 1.0
O1 I:CO3502 4.1 47.3 1.0
CA I:ASP194 4.2 34.9 1.0
HG12 I:ILE165 4.2 47.4 1.0
CG I:GLU195 4.2 44.3 1.0
CB I:ASP194 4.3 35.4 1.0
HE1 I:HIS288 4.3 51.0 1.0
CB I:GLU195 4.3 43.3 1.0
HD3 I:PRO196 4.3 45.9 1.0
HZ2 I:LYS167 4.4 42.1 1.0
C1 I:CAP500 4.4 36.0 1.0
C4 I:CAP500 4.4 33.6 1.0
CE1 I:HIS288 4.4 42.5 1.0
H4 I:CAP500 4.5 40.4 1.0
C I:ASP194 4.5 35.5 1.0
CG2 I:ILE165 4.5 39.0 1.0
CA I:GLU195 4.7 41.1 1.0
H51 I:CAP500 4.7 40.1 1.0
HB3 I:ASP194 4.7 42.4 1.0
HG3 I:LYS169 4.7 49.8 1.0
HG3 I:GLU195 4.8 53.1 1.0
O1 I:CAP500 4.8 36.6 1.0
HG2 I:GLU195 4.8 53.1 1.0
HG23 I:ILE165 4.8 46.8 1.0
H12 I:CAP500 4.9 43.2 1.0
CD2 I:HIS288 4.9 42.1 1.0
CG J:ASN112 5.0 32.8 1.0
HB2 I:ASP194 5.0 42.4 1.0
HG22 I:ILE165 5.0 46.8 1.0
O J:HOH687 5.0 33.6 1.0
CE I:LYS169 5.0 41.4 1.0
C5 I:CAP500 5.0 33.4 1.0

Magnesium binding site 10 out of 12 in 5koz

Go back to Magnesium Binding Sites List in 5koz
Magnesium binding site 10 out of 12 in the Structure Function Studies of R. Palustris Rubisco (K192C 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 (K192C Mutant; Cabp-Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg501

b:44.9
occ:1.00
O2 J:CO3502 1.9 42.6 1.0
OD1 J:ASP194 2.0 40.2 1.0
HO2 J:CAP500 2.0 51.9 1.0
O6 J:CAP500 2.1 41.5 1.0
OE1 J:GLU195 2.1 40.1 1.0
O2 J:CAP500 2.1 43.2 1.0
O3 J:CAP500 2.3 36.0 1.0
C2 J:CAP500 2.8 39.1 1.0
C J:CAP500 2.8 39.0 1.0
HO3 J:CAP500 2.9 43.1 1.0
HD21 I:ASN112 3.0 43.7 1.0
C J:CO3502 3.1 38.3 1.0
H J:GLU195 3.1 40.9 1.0
CG J:ASP194 3.1 36.6 1.0
C3 J:CAP500 3.1 37.6 1.0
HZ3 J:LYS169 3.1 53.2 1.0
CD J:GLU195 3.2 36.1 1.0
HZ1 J:LYS169 3.3 53.2 1.0
HZ3 J:LYS167 3.3 41.8 1.0
HG21 J:ILE165 3.4 40.5 1.0
HZ2 J:LYS169 3.5 53.2 1.0
HZ1 J:LYS167 3.5 41.8 1.0
NZ J:LYS169 3.5 44.3 1.0
HA J:ASP194 3.5 40.6 1.0
HE2 J:HIS288 3.5 42.8 1.0
O3 J:CO3502 3.5 35.1 1.0
OE2 J:GLU195 3.6 36.5 1.0
H3 J:CAP500 3.6 45.1 1.0
OD2 J:ASP194 3.6 37.5 1.0
ND2 I:ASN112 3.7 36.4 1.0
HD22 I:ASN112 3.7 43.7 1.0
NZ J:LYS167 3.8 34.8 1.0
N J:GLU195 3.9 34.0 1.0
O7 J:CAP500 4.0 38.9 1.0
HB3 J:GLU195 4.1 40.5 1.0
NE2 J:HIS288 4.1 35.7 1.0
HZ2 J:LYS167 4.1 41.8 1.0
O1 J:CO3502 4.1 38.9 1.0
HG12 J:ILE165 4.1 42.1 1.0
CA J:ASP194 4.2 33.8 1.0
C1 J:CAP500 4.2 38.5 1.0
CB J:ASP194 4.2 34.4 1.0
C4 J:CAP500 4.3 37.7 1.0
CG2 J:ILE165 4.4 33.7 1.0
H4 J:CAP500 4.4 45.3 1.0
CG J:GLU195 4.5 34.8 1.0
HD3 J:PRO196 4.5 38.0 1.0
HE1 J:HIS288 4.5 43.5 1.0
O1 J:CAP500 4.5 38.2 1.0
C J:ASP194 4.6 34.4 1.0
CB J:GLU195 4.6 33.7 1.0
CE1 J:HIS288 4.6 36.2 1.0
H12 J:CAP500 4.7 46.2 1.0
HG3 J:LYS169 4.7 52.8 1.0
HB3 J:ASP194 4.7 41.2 1.0
HG23 J:ILE165 4.7 40.5 1.0
H52 J:CAP500 4.8 43.2 1.0
HB2 J:ASP194 4.9 41.2 1.0
HG22 J:ILE165 4.9 40.5 1.0
H11 J:CAP500 4.9 46.2 1.0
CA J:GLU195 4.9 32.8 1.0
CG I:ASN112 4.9 37.1 1.0
CE J:LYS169 4.9 45.1 1.0
CG1 J:ILE165 5.0 35.1 1.0
HG3 J:GLU195 5.0 41.7 1.0

Reference:

M.A.Arbing, J.A.North, S.Satagopan, V.A.Varaljay, A.Shin, F.R.Tabita. Structure Function Studies of R. Palustris Rubisco. To Be Published.
Page generated: Mon Dec 14 20:38:13 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