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Molybdenum in PDB 7ut9: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Adp/Atp-Bound) During Catalytic N2 Reduction

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

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

Other elements in 7ut9:

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

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

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Adp/Atp-Bound) During Catalytic N2 Reduction (pdb code 7ut9). 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, Adp/Atp-Bound) During Catalytic N2 Reduction, PDB code: 7ut9:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 7ut9

Go back to Molybdenum Binding Sites List in 7ut9
Molybdenum binding site 1 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Adp/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, Adp/Atp-Bound) During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo502

b:20.9
occ:1.00
MO1 A:ICS502 0.0 20.9 1.0
S1B A:ICS502 2.3 31.1 1.0
S4B A:ICS502 2.3 27.1 1.0
S3B A:ICS502 2.4 26.7 1.0
ND1 A:HIS442 2.5 22.0 1.0
FE6 A:ICS502 2.7 30.1 1.0
FE7 A:ICS502 2.7 32.3 1.0
O7 A:HCA501 2.7 34.7 1.0
FE5 A:ICS502 2.7 18.9 1.0
O6 A:HCA501 2.7 27.5 1.0
CG A:HIS442 3.5 20.4 1.0
CE1 A:HIS442 3.5 25.7 1.0
CX A:ICS502 3.5 34.0 1.0
CB A:HIS442 3.6 28.4 1.0
C7 A:HCA501 3.6 34.6 1.0
C3 A:HCA501 3.7 36.8 1.0
C5 A:HCA501 4.3 35.2 1.0
CA A:HIS442 4.5 22.2 1.0
O1 A:HCA501 4.5 35.7 1.0
NE2 A:HIS442 4.6 20.8 1.0
C4 A:HCA501 4.6 36.5 1.0
CD2 A:HIS442 4.6 18.9 1.0
S2B A:ICS502 4.8 18.1 1.0
C2 A:HCA501 4.8 37.0 1.0
S5A A:ICS502 4.8 13.9 1.0
O5 A:HCA501 4.8 38.0 1.0
S3A A:ICS502 4.9 25.4 1.0

Molybdenum binding site 2 out of 2 in 7ut9

Go back to Molybdenum Binding Sites List in 7ut9
Molybdenum binding site 2 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Adp/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, Adp/Atp-Bound) During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo502

b:46.8
occ:1.00
MO1 C:ICS502 0.0 46.8 1.0
S1B C:ICS502 2.3 69.0 1.0
S4B C:ICS502 2.3 64.2 1.0
S3B C:ICS502 2.4 59.1 1.0
ND1 C:HIS442 2.6 50.1 1.0
FE6 C:ICS502 2.7 69.0 1.0
FE7 C:ICS502 2.7 69.0 1.0
FE5 C:ICS502 2.7 44.7 1.0
O7 C:HCA501 2.8 62.4 1.0
O6 C:HCA501 2.8 60.5 1.0
CE1 C:HIS442 3.5 53.7 1.0
CX C:ICS502 3.5 58.6 1.0
CG C:HIS442 3.6 51.3 1.0
C7 C:HCA501 3.7 60.9 1.0
CB C:HIS442 3.8 53.3 1.0
C3 C:HCA501 3.8 62.1 1.0
O2 C:HCA501 4.0 58.8 1.0
C5 C:HCA501 4.5 55.2 1.0
NE2 C:HIS442 4.6 55.9 1.0
C1 C:HCA501 4.7 60.2 1.0
CD2 C:HIS442 4.7 53.2 1.0
S2B C:ICS502 4.8 64.6 1.0
CA C:HIS442 4.8 50.4 1.0
C4 C:HCA501 4.8 58.5 1.0
C2 C:HCA501 4.8 58.6 1.0
S5A C:ICS502 4.8 65.4 1.0
NE C:ARG96 4.8 25.9 1.0
NH1 C:ARG359 4.8 59.4 1.0
O5 C:HCA501 4.9 59.3 1.0
S3A C:ICS502 4.9 62.1 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 17:02:58 2024

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