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Molybdenum in PDB 8e3t: Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation

Enzymatic activity of Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation

All present enzymatic activity of Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation:
1.18.6.1;

Protein crystallography data

The structure of Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3t was solved by H.L.Rutledge, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.13 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 76.607, 127.968, 107.269, 90, 108.85, 90
R / Rfree (%) 22.3 / 24.3

Other elements in 8e3t:

The structure of Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation also contains other interesting chemical elements:

Sodium (Na) 2 atoms
Iron (Fe) 30 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation (pdb code 8e3t). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3t:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 8e3t

Go back to Molybdenum Binding Sites List in 8e3t
Molybdenum binding site 1 out of 2 in the Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo502

b:25.1
occ:1.00
MO1 A:ICS502 0.0 25.1 1.0
S1B A:ICS502 2.3 29.0 1.0
S4B A:ICS502 2.4 29.0 1.0
S3B A:ICS502 2.4 30.3 1.0
O7 A:HCA501 2.4 29.9 1.0
ND1 A:HIS442 2.6 27.7 1.0
O6 A:HCA501 2.6 26.8 1.0
FE6 A:ICS502 2.7 25.2 1.0
FE7 A:ICS502 2.7 31.0 1.0
FE5 A:ICS502 2.7 22.9 1.0
C7 A:HCA501 3.2 28.3 1.0
HE1 A:HIS442 3.3 34.2 1.0
CE1 A:HIS442 3.3 28.5 1.0
C3 A:HCA501 3.3 28.9 1.0
CX A:ICS502 3.5 25.2 1.0
H52 A:HCA501 3.5 33.6 1.0
HB3 A:HIS442 3.6 31.5 1.0
CG A:HIS442 3.7 26.6 1.0
O A:HOH675 3.9 25.3 1.0
H22 A:HCA501 4.0 36.4 1.0
CB A:HIS442 4.1 26.2 1.0
HA A:HIS442 4.1 29.4 1.0
HE A:ARG96 4.2 33.3 1.0
C2 A:HCA501 4.3 30.3 1.0
O5 A:HCA501 4.3 30.2 1.0
C4 A:HCA501 4.4 29.7 1.0
C5 A:HCA501 4.4 28.0 1.0
NE2 A:HIS442 4.5 28.3 1.0
H41 A:HCA501 4.6 35.7 1.0
HG22 A:ILE355 4.6 35.7 1.0
CA A:HIS442 4.7 24.4 1.0
HA3 A:GLY356 4.7 34.5 1.0
CD2 A:HIS442 4.7 27.4 1.0
O A:HOH743 4.7 34.9 1.0
S2B A:ICS502 4.8 29.2 1.0
O2 A:HCA501 4.8 32.8 1.0
S5A A:ICS502 4.8 25.5 1.0
S3A A:ICS502 4.9 27.2 1.0
HB2 A:HIS442 5.0 31.5 1.0
H A:GLY356 5.0 35.0 1.0

Molybdenum binding site 2 out of 2 in 8e3t

Go back to Molybdenum Binding Sites List in 8e3t
Molybdenum binding site 2 out of 2 in the Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo502

b:52.5
occ:1.00
MO1 C:ICS502 0.0 52.5 1.0
S1B C:ICS502 2.3 30.9 1.0
S4B C:ICS502 2.3 31.5 1.0
S3B C:ICS502 2.4 36.5 1.0
O7 C:HCA501 2.4 32.2 1.0
O5 C:HCA501 2.5 28.4 1.0
ND1 C:HIS442 2.6 29.1 1.0
FE7 C:ICS502 2.7 32.3 1.0
FE6 C:ICS502 2.7 27.6 1.0
FE5 C:ICS502 2.7 26.7 1.0
C7 C:HCA501 3.3 29.7 1.0
HB3 C:HIS442 3.3 32.3 1.0
C3 C:HCA501 3.4 32.0 1.0
CE1 C:HIS442 3.4 29.8 1.0
HE1 C:HIS442 3.5 35.7 1.0
CX C:ICS502 3.5 26.3 1.0
H52 C:HCA501 3.6 34.7 1.0
CG C:HIS442 3.6 27.8 1.0
O C:HOH687 3.9 27.2 1.0
CB C:HIS442 3.9 26.9 1.0
HA C:HIS442 4.0 31.5 1.0
H22 C:HCA501 4.3 38.6 1.0
O1 C:HCA501 4.3 33.7 1.0
C2 C:HCA501 4.4 32.1 1.0
C4 C:HCA501 4.4 30.5 1.0
O6 C:HCA501 4.4 30.9 1.0
C5 C:HCA501 4.5 28.9 1.0
HG22 C:ILE355 4.5 34.5 1.0
HD2 C:ARG96 4.5 35.5 1.0
CA C:HIS442 4.6 26.2 1.0
NE2 C:HIS442 4.6 29.4 1.0
H41 C:HCA501 4.7 36.6 1.0
CD2 C:HIS442 4.7 28.2 1.0
HB2 C:HIS442 4.8 32.3 1.0
S2B C:ICS502 4.8 27.8 1.0
S5A C:ICS502 4.8 24.4 1.0
C1 C:HCA501 4.8 33.7 1.0
HH11 C:ARG96 4.8 34.6 1.0
HA3 C:GLY356 4.9 36.2 1.0
S3A C:ICS502 4.9 28.7 1.0
HD3 C:ARG96 4.9 35.5 1.0

Reference:

H.L.Rutledge, M.J.Field, J.Rittle, M.T.Green, F.A.Tezcan. Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster. J.Am.Chem.Soc. V. 144 22101 2022.
ISSN: ESSN 1520-5126
PubMed: 36445204
DOI: 10.1021/JACS.2C09480
Page generated: Sun Aug 17 04:32:10 2025

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