Atomistry » Magnesium » PDB 1lnz-1mez » 1m3u
Atomistry »
  Magnesium »
    PDB 1lnz-1mez »
      1m3u »

Magnesium in PDB 1m3u: Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate

Enzymatic activity of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate

All present enzymatic activity of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate:
2.1.2.11;

Protein crystallography data

The structure of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate, PDB code: 1m3u was solved by F.Von Delft, T.Inoue, S.A.Saldanha, H.H.Ottenhof, V.Dhanaraj, M.Witty, C.Abell, A.G.Smith, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 86.074, 157.170, 100.181, 90.00, 97.44, 90.00
R / Rfree (%) 15.2 / 19.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate (pdb code 1m3u). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 10 binding sites of Magnesium where determined in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate, PDB code: 1m3u:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 1 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg266

b:40.6
occ:1.00
 O3 A:KPL265 2.2 31.5 1.0
OD2 A:ASP84 2.3 30.3 1.0
O2 A:KPL265 2.4 42.8 1.0
O A:HOH267 2.5 31.7 1.0
OD1 A:ASP45 2.5 24.0 1.0
O A:HOH268 2.5 36.9 1.0
C5 A:KPL265 3.0 40.1 1.0
C6 A:KPL265 3.0 38.1 1.0
CG A:ASP84 3.3 27.5 1.0
NZ A:LYS112 3.4 24.0 1.0
O A:HOH269 3.4 35.2 1.0
CG A:ASP45 3.5 27.1 1.0
N A:ASP45 3.8 23.5 1.0
OD1 A:ASP84 3.8 25.3 1.0
O1 A:KPL265 3.8 31.2 0.5
OD2 A:ASP45 4.1 26.9 1.0
OE2 A:GLU114 4.1 33.0 1.0
N A:SER46 4.2 22.9 1.0
O4 A:KPL265 4.2 36.3 1.0
C2 A:KPL265 4.4 38.2 0.5
CA A:ASP45 4.4 23.3 1.0
C2 A:KPL265 4.4 40.9 0.5
CA A:GLY44 4.4 24.4 1.0
CB A:ASP45 4.5 24.1 1.0
C A:GLY44 4.5 23.6 1.0
CB A:ASP84 4.6 24.3 1.0
CE A:LYS112 4.6 26.6 1.0
CE1 A:HIS136 4.6 26.7 1.0
C A:ASP45 4.6 22.1 1.0
C4 A:KPL265 4.6 36.9 0.5
C4 A:KPL265 4.7 41.5 0.5
O A:HOH270 4.7 34.5 1.0
ND1 A:HIS136 4.8 25.9 1.0
C3 A:KPL265 4.9 41.4 0.5
C3 A:KPL265 5.0 38.2 0.5
CD2 A:LEU42 5.0 32.1 1.0

Magnesium binding site 2 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 2 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg266

b:37.6
occ:1.00
 OD2 B:ASP84 2.2 25.6 1.0
O3 B:KPL265 2.3 32.3 1.0
O B:HOH267 2.4 32.6 1.0
OD1 B:ASP45 2.4 26.4 1.0
O B:HOH268 2.5 35.6 1.0
O2 B:KPL265 2.6 39.7 1.0
C6 B:KPL265 3.0 36.7 1.0
C5 B:KPL265 3.1 36.9 1.0
CG B:ASP84 3.3 27.4 1.0
CG B:ASP45 3.4 27.1 1.0
NZ B:LYS112 3.4 22.6 1.0
O B:HOH269 3.5 34.0 1.0
N B:ASP45 3.7 23.6 1.0
OD1 B:ASP84 3.7 27.9 1.0
OD2 B:ASP45 4.0 28.9 1.0
OE2 B:GLU114 4.1 33.0 1.0
O1 B:KPL265 4.2 30.7 0.5
O4 B:KPL265 4.2 35.2 1.0
N B:SER46 4.2 21.5 1.0
CB B:ASP45 4.4 23.8 1.0
CA B:ASP45 4.4 23.1 1.0
C2 B:KPL265 4.4 36.4 0.5
CB B:ASP84 4.5 24.7 1.0
C2 B:KPL265 4.5 38.3 0.5
CA B:GLY44 4.5 25.1 1.0
C B:GLY44 4.6 24.5 1.0
C B:ASP45 4.6 21.4 1.0
CE1 B:HIS136 4.7 23.8 1.0
CE B:LYS112 4.7 25.9 1.0
O B:HOH270 4.8 32.8 1.0
C4 B:KPL265 4.8 34.5 0.5
C4 B:KPL265 4.8 38.8 0.5
ND1 B:HIS136 4.9 24.4 1.0
C3 B:KPL265 4.9 39.4 0.5

Magnesium binding site 3 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 3 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg266

b:47.7
occ:1.00
 OD2 C:ASP84 2.2 29.5 1.0
O3 C:KPL265 2.2 32.0 1.0
OD1 C:ASP45 2.4 25.5 1.0
O C:HOH267 2.4 34.5 1.0
O C:HOH268 2.5 35.0 1.0
O2 C:KPL265 2.6 41.2 1.0
C6 C:KPL265 3.0 40.3 1.0
C5 C:KPL265 3.2 41.9 1.0
CG C:ASP84 3.3 27.1 1.0
CG C:ASP45 3.4 28.5 1.0
NZ C:LYS112 3.5 24.4 1.0
O C:HOH269 3.6 30.4 1.0
N C:ASP45 3.7 24.1 1.0
OD1 C:ASP84 3.8 28.1 1.0
O1 C:KPL265 3.8 37.8 0.5
OD2 C:ASP45 4.0 29.1 1.0
OE2 C:GLU114 4.0 32.4 1.0
N C:SER46 4.1 22.9 1.0
O4 C:KPL265 4.2 38.6 1.0
CA C:ASP45 4.3 24.9 1.0
CB C:ASP45 4.3 24.8 1.0
CA C:GLY44 4.4 24.0 1.0
C C:GLY44 4.4 24.1 1.0
CB C:ASP84 4.4 24.8 1.0
C C:ASP45 4.5 23.5 1.0
C2 C:KPL265 4.5 41.7 0.5
C2 C:KPL265 4.5 41.8 0.5
C4 C:KPL265 4.7 40.6 0.5
CE C:LYS112 4.7 25.8 1.0
CE1 C:HIS136 4.7 24.1 1.0
O C:HOH270 4.8 32.6 1.0
C4 C:KPL265 4.9 42.0 0.5
ND1 C:HIS136 4.9 25.0 1.0

Magnesium binding site 4 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 4 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg266

b:46.7
occ:1.00
 OD2 D:ASP84 2.1 28.9 1.0
O3 D:KPL265 2.2 29.3 1.0
O D:HOH267 2.5 35.1 1.0
O D:HOH268 2.5 40.0 1.0
OD1 D:ASP45 2.6 24.6 1.0
O2 D:KPL265 2.6 44.9 1.0
C6 D:KPL265 3.0 40.3 1.0
C5 D:KPL265 3.1 40.6 1.0
CG D:ASP84 3.2 26.9 1.0
NZ D:LYS112 3.4 22.5 1.0
CG D:ASP45 3.5 25.7 1.0
O D:HOH269 3.6 30.3 1.0
OD1 D:ASP84 3.6 27.4 1.0
N D:ASP45 3.6 25.0 1.0
O1 D:KPL265 4.0 36.2 0.5
OE2 D:GLU114 4.1 30.6 1.0
OD2 D:ASP45 4.1 27.3 1.0
N D:SER46 4.2 22.7 1.0
O4 D:KPL265 4.2 38.3 1.0
CA D:GLY44 4.3 26.0 1.0
CA D:ASP45 4.4 24.6 1.0
CB D:ASP84 4.4 24.4 1.0
C D:GLY44 4.4 25.3 1.0
CB D:ASP45 4.5 25.0 1.0
C2 D:KPL265 4.5 40.2 0.5
C2 D:KPL265 4.5 40.4 0.5
C D:ASP45 4.6 23.7 1.0
CE D:LYS112 4.6 24.1 1.0
CE1 D:HIS136 4.7 25.3 1.0
O D:HOH270 4.8 33.0 1.0
C4 D:KPL265 4.8 39.3 0.5
ND1 D:HIS136 4.9 24.4 1.0
CD2 D:LEU42 4.9 32.7 1.0
C4 D:KPL265 5.0 39.4 0.5

Magnesium binding site 5 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 5 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg266

b:36.9
occ:1.00
 O3 E:KPL265 2.2 26.2 1.0
OD2 E:ASP84 2.4 21.2 1.0
OD1 E:ASP45 2.4 20.9 1.0
O2 E:KPL265 2.5 37.8 1.0
O E:HOH268 2.6 29.6 1.0
O E:HOH267 2.8 29.3 1.0
C6 E:KPL265 3.0 35.5 1.0
C5 E:KPL265 3.1 37.4 1.0
CG E:ASP45 3.4 22.7 1.0
CG E:ASP84 3.5 23.9 1.0
O E:HOH269 3.6 24.3 1.0
NZ E:LYS112 3.6 18.1 1.0
N E:ASP45 3.7 21.9 1.0
OD1 E:ASP84 3.9 27.2 1.0
N E:SER46 4.0 20.9 1.0
O1 E:KPL265 4.0 35.1 0.5
OD2 E:ASP45 4.1 26.6 1.0
O4 E:KPL265 4.2 38.3 1.0
CA E:ASP45 4.3 21.3 1.0
CA E:GLY44 4.3 21.5 1.0
C2 E:KPL265 4.4 37.6 0.5
OE2 E:GLU114 4.4 25.1 1.0
CB E:ASP45 4.4 22.3 1.0
C2 E:KPL265 4.4 38.8 0.5
C E:GLY44 4.4 22.0 1.0
C E:ASP45 4.5 20.6 1.0
C4 E:KPL265 4.5 37.5 0.5
CB E:ASP84 4.6 20.8 1.0
CE E:LYS112 4.7 19.8 1.0
C4 E:KPL265 4.7 39.5 0.5
CE1 E:HIS136 4.8 19.2 1.0
CD2 E:LEU42 4.9 22.4 1.0
C3 E:KPL265 4.9 39.1 0.5
ND1 E:HIS136 5.0 19.0 1.0
CA E:SER46 5.0 20.3 1.0

Magnesium binding site 6 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 6 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg266

b:39.3
occ:1.00
 O3 F:KPL265 2.3 34.8 1.0
OD2 F:ASP84 2.3 23.7 1.0
O2 F:KPL265 2.4 38.3 1.0
O F:HOH267 2.5 35.1 1.0
OD1 F:ASP45 2.6 25.9 1.0
O F:HOH268 2.7 33.0 1.0
C6 F:KPL265 3.0 38.8 1.0
C5 F:KPL265 3.0 37.9 1.0
CG F:ASP84 3.3 25.2 1.0
NZ F:LYS112 3.3 23.2 1.0
O F:HOH269 3.6 28.7 1.0
CG F:ASP45 3.6 24.8 1.0
N F:ASP45 3.7 24.6 1.0
OD1 F:ASP84 3.7 30.4 1.0
O1 F:KPL265 4.1 30.1 0.5
OE2 F:GLU114 4.1 32.6 1.0
N F:SER46 4.2 21.7 1.0
O4 F:KPL265 4.2 40.3 1.0
OD2 F:ASP45 4.3 28.2 1.0
CA F:GLY44 4.3 24.1 1.0
C2 F:KPL265 4.4 36.5 0.5
C2 F:KPL265 4.4 38.3 0.5
CA F:ASP45 4.4 23.5 1.0
CE F:LYS112 4.4 25.4 1.0
C F:GLY44 4.5 24.7 1.0
CB F:ASP84 4.5 24.1 1.0
CB F:ASP45 4.5 24.4 1.0
C4 F:KPL265 4.6 35.8 0.5
C F:ASP45 4.6 22.5 1.0
CE1 F:HIS136 4.7 24.7 1.0
C4 F:KPL265 4.8 39.2 0.5
CD2 F:LEU42 4.8 27.1 1.0
O F:HOH270 4.8 30.8 1.0
ND1 F:HIS136 4.8 23.8 1.0
C3 F:KPL265 4.9 38.2 0.5
C3 F:KPL265 5.0 37.8 0.5

Magnesium binding site 7 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 7 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg266

b:43.5
occ:1.00
 OD2 G:ASP84 2.2 27.0 1.0
O3 G:KPL265 2.3 30.2 1.0
O2 G:KPL265 2.4 41.2 1.0
O G:HOH267 2.4 36.4 1.0
O G:HOH268 2.5 47.5 1.0
OD1 G:ASP45 2.7 28.2 1.0
C6 G:KPL265 3.1 43.5 1.0
C5 G:KPL265 3.1 41.6 1.0
NZ G:LYS112 3.3 22.8 1.0
CG G:ASP84 3.3 26.6 1.0
O G:HOH269 3.6 40.7 1.0
OD1 G:ASP84 3.7 29.0 1.0
CG G:ASP45 3.7 29.4 1.0
N G:ASP45 3.8 24.6 1.0
O1 G:KPL265 4.0 41.5 0.5
OE2 G:GLU114 4.0 36.5 1.0
O4 G:KPL265 4.3 42.0 1.0
N G:SER46 4.3 25.1 1.0
OD2 G:ASP45 4.3 30.5 1.0
CA G:GLY44 4.4 25.6 1.0
C2 G:KPL265 4.5 40.7 0.5
C2 G:KPL265 4.5 41.7 0.5
C G:GLY44 4.5 25.6 1.0
CA G:ASP45 4.5 24.9 1.0
CE G:LYS112 4.5 25.7 1.0
CB G:ASP84 4.6 23.9 1.0
O G:HOH270 4.6 38.7 1.0
CB G:ASP45 4.6 25.6 1.0
CE1 G:HIS136 4.6 28.4 1.0
C G:ASP45 4.8 23.5 1.0
ND1 G:HIS136 4.8 27.3 1.0
C4 G:KPL265 4.9 41.6 0.5
C3 G:KPL265 4.9 39.7 0.5
C3 G:KPL265 4.9 42.0 0.5

Magnesium binding site 8 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 8 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg266

b:36.9
occ:1.00
 OD2 H:ASP84 2.1 26.4 1.0
O3 H:KPL265 2.1 30.2 1.0
O2 H:KPL265 2.4 41.6 1.0
OD1 H:ASP45 2.5 25.5 1.0
O H:HOH268 2.6 38.8 1.0
O H:HOH267 2.7 41.5 1.0
C6 H:KPL265 2.9 38.3 1.0
C5 H:KPL265 3.0 39.6 1.0
CG H:ASP84 3.2 27.1 1.0
NZ H:LYS112 3.4 21.2 1.0
O H:HOH269 3.5 35.3 1.0
CG H:ASP45 3.5 24.5 1.0
OD1 H:ASP84 3.6 28.1 1.0
N H:ASP45 3.7 24.5 1.0
O1 H:KPL265 4.0 36.6 0.5
O4 H:KPL265 4.1 38.1 1.0
N H:SER46 4.1 23.0 1.0
OD2 H:ASP45 4.2 26.8 1.0
CA H:GLY44 4.3 24.7 1.0
OE2 H:GLU114 4.3 27.0 1.0
C2 H:KPL265 4.3 39.0 0.5
CA H:ASP45 4.3 23.7 1.0
CB H:ASP84 4.4 23.9 1.0
C H:GLY44 4.4 24.6 1.0
C2 H:KPL265 4.4 40.2 0.5
CB H:ASP45 4.5 24.3 1.0
C4 H:KPL265 4.6 39.1 0.5
C H:ASP45 4.6 22.2 1.0
CE H:LYS112 4.6 23.9 1.0
CD2 H:LEU42 4.8 33.6 1.0
CE1 H:HIS136 4.9 23.8 1.0
O H:HOH270 4.9 33.8 1.0
C3 H:KPL265 4.9 39.8 0.5
C4 H:KPL265 4.9 40.2 0.5
C3 H:KPL265 5.0 38.1 0.5

Magnesium binding site 9 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 9 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg266

b:50.3
occ:1.00
 OD2 I:ASP84 2.2 32.1 1.0
O3 I:KPL265 2.2 35.3 1.0
O I:HOH267 2.3 29.1 1.0
O I:HOH268 2.4 29.4 1.0
OD1 I:ASP45 2.5 26.5 1.0
O2 I:KPL265 2.5 40.7 1.0
C6 I:KPL265 3.0 39.9 1.0
C5 I:KPL265 3.1 39.9 1.0
NZ I:LYS112 3.2 25.4 1.0
CG I:ASP84 3.3 26.2 1.0
CG I:ASP45 3.4 23.6 1.0
O I:HOH269 3.5 30.6 1.0
N I:ASP45 3.6 24.1 1.0
OD1 I:ASP84 3.7 28.4 1.0
OE2 I:GLU114 3.9 27.8 1.0
O1 I:KPL265 4.0 34.5 0.5
OD2 I:ASP45 4.0 27.6 1.0
N I:SER46 4.2 21.6 1.0
O4 I:KPL265 4.2 38.8 1.0
CA I:ASP45 4.3 22.6 1.0
CB I:ASP45 4.4 23.7 1.0
CA I:GLY44 4.4 23.6 1.0
CB I:ASP84 4.4 23.5 1.0
C I:GLY44 4.4 24.7 1.0
C2 I:KPL265 4.4 37.7 0.5
C2 I:KPL265 4.4 39.0 0.5
CE I:LYS112 4.5 29.6 1.0
C I:ASP45 4.6 22.6 1.0
CE1 I:HIS136 4.6 24.9 1.0
C4 I:KPL265 4.6 35.1 0.5
O I:HOH270 4.7 34.4 1.0
ND1 I:HIS136 4.8 24.3 1.0
C4 I:KPL265 4.8 39.3 0.5
O I:HOH528 4.8 40.1 1.0
C3 I:KPL265 4.9 39.8 0.5

Magnesium binding site 10 out of 10 in 1m3u

Go back to Magnesium Binding Sites List in 1m3u
Magnesium binding site 10 out of 10 in the Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Crystal Structure of Ketopantoate Hydroxymethyltransferase Complexed the Product Ketopantoate within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg266

b:37.1
occ:1.00
 OD2 J:ASP84 2.1 19.6 1.0
O3 J:KPL265 2.3 29.7 1.0
O2 J:KPL265 2.4 38.6 1.0
O J:HOH267 2.5 41.4 1.0
O J:HOH268 2.7 34.9 1.0
OD1 J:ASP45 2.8 20.3 1.0
C6 J:KPL265 3.1 37.8 1.0
C5 J:KPL265 3.1 38.3 1.0
CG J:ASP84 3.3 20.4 1.0
NZ J:LYS112 3.3 19.8 1.0
OD1 J:ASP84 3.7 22.6 1.0
CG J:ASP45 3.7 22.8 1.0
N J:ASP45 3.8 21.8 1.0
O J:HOH269 3.8 26.2 1.0
O1 J:KPL265 3.9 37.7 0.5
OE2 J:GLU114 4.2 34.1 1.0
OD2 J:ASP45 4.3 27.4 1.0
O4 J:KPL265 4.3 38.8 1.0
CA J:GLY44 4.3 22.4 1.0
N J:SER46 4.3 20.9 1.0
C2 J:KPL265 4.5 39.0 0.5
C J:GLY44 4.5 22.0 1.0
CB J:ASP84 4.5 20.1 1.0
C2 J:KPL265 4.5 39.7 0.5
CE J:LYS112 4.5 20.9 1.0
CA J:ASP45 4.6 21.1 1.0
CE1 J:HIS136 4.6 24.1 1.0
CB J:ASP45 4.6 20.3 1.0
ND1 J:HIS136 4.8 24.3 1.0
C4 J:KPL265 4.8 38.8 0.5
C J:ASP45 4.8 21.1 1.0
C3 J:KPL265 4.9 39.8 0.5
O J:HOH270 4.9 25.9 1.0
C3 J:KPL265 5.0 38.8 0.5

Reference:

F.Von Delft, T.Inoue, S.A.Saldanha, H.H.Ottenhof, F.Schmitzberger, L.M.Birch, V.Dhanaraj, M.Witty, A.G.Smith, T.L.Blundell, C.Abell. Structure of E. Coli Ketopantoate Hydroxymethyl Transferase Complexed with Ketopantoate and Mg(2+), Solved By Locating 160 Selenomethionine Sites. Structure V. 11 985 2003.
ISSN: ISSN 0969-2126
PubMed: 12906829
DOI: 10.1016/S0969-2126(03)00158-8
Page generated: Tue Aug 13 08:37:04 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy