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Molybdenum in PDB 7ut8: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction

Enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction

All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction:
1.18.6.1;

Other elements in 7ut8:

The structure of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Iron (Fe) 36 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction (pdb code 7ut8). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction, PDB code: 7ut8:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 7ut8

Go back to Molybdenum Binding Sites List in 7ut8
Molybdenum binding site 1 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo502

b:20.0
occ:1.00
MO1 A:ICS502 0.0 20.0 1.0
S1B A:ICS502 2.3 32.7 1.0
S4B A:ICS502 2.3 27.5 1.0
S3B A:ICS502 2.4 23.3 1.0
ND1 A:HIS442 2.6 19.7 1.0
O7 A:HCA501 2.6 28.9 1.0
FE6 A:ICS502 2.7 23.3 1.0
FE7 A:ICS502 2.7 24.4 1.0
FE5 A:ICS502 2.7 22.6 1.0
O6 A:HCA501 2.7 22.4 1.0
CE1 A:HIS442 3.5 25.0 1.0
CX A:ICS502 3.5 35.3 1.0
CG A:HIS442 3.5 16.5 1.0
C7 A:HCA501 3.6 28.7 1.0
C3 A:HCA501 3.7 31.5 1.0
CB A:HIS442 3.7 27.3 1.0
O1 A:HCA501 4.1 25.6 1.0
C5 A:HCA501 4.3 25.7 1.0
CA A:HIS442 4.5 18.8 1.0
C4 A:HCA501 4.6 29.9 1.0
NE2 A:HIS442 4.7 19.4 1.0
CD2 A:HIS442 4.7 15.3 1.0
C2 A:HCA501 4.7 30.3 1.0
S2B A:ICS502 4.8 19.2 1.0
O5 A:HCA501 4.8 28.7 1.0
S5A A:ICS502 4.8 15.7 1.0
C1 A:HCA501 4.9 27.3 1.0
S3A A:ICS502 4.9 27.8 1.0

Molybdenum binding site 2 out of 2 in 7ut8

Go back to Molybdenum Binding Sites List in 7ut8
Molybdenum binding site 2 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo502

b:47.1
occ:1.00
MO1 C:ICS502 0.0 47.1 1.0
S1B C:ICS502 2.3 58.9 1.0
S4B C:ICS502 2.3 51.6 1.0
S3B C:ICS502 2.4 53.4 1.0
O7 C:HCA501 2.6 51.0 1.0
ND1 C:HIS442 2.6 43.0 1.0
FE6 C:ICS502 2.7 81.2 1.0
FE7 C:ICS502 2.7 64.7 1.0
FE5 C:ICS502 2.7 39.2 1.0
O6 C:HCA501 2.7 53.5 1.0
CX C:ICS502 3.5 60.6 1.0
CE1 C:HIS442 3.6 47.3 1.0
CG C:HIS442 3.6 49.4 1.0
C7 C:HCA501 3.6 53.8 1.0
C3 C:HCA501 3.7 55.4 1.0
CB C:HIS442 3.8 47.4 1.0
C5 C:HCA501 4.4 50.0 1.0
O2 C:HCA501 4.5 52.5 1.0
C4 C:HCA501 4.6 54.6 1.0
NE2 C:HIS442 4.7 49.1 1.0
C2 C:HCA501 4.7 53.1 1.0
CD2 C:HIS442 4.8 50.7 1.0
S2B C:ICS502 4.8 60.7 1.0
S5A C:ICS502 4.8 59.6 1.0
O5 C:HCA501 4.8 51.2 1.0
C1 C:HCA501 4.9 53.3 1.0
S3A C:ICS502 4.9 55.6 1.0

Reference:

H.L.Rutledge, B.D.Cook, H.P.M.Nguyen, M.A.Herzik Jr., F.A.Tezcan. Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641
Page generated: Sun Oct 6 17:02:40 2024

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