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Molybdenum in PDB 3min: Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State

Enzymatic activity of Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State

All present enzymatic activity of Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State:
1.18.6.1;

Protein crystallography data

The structure of Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State, PDB code: 3min was solved by J.W.Peters, M.H.B.Stowell, S.M.Soltis, M.W.Day, J.Kim, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.03
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 108.000, 131.300, 81.000, 90.00, 110.70, 90.00
R / Rfree (%) 20.6 / 26.4

Other elements in 3min:

The structure of Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State also contains other interesting chemical elements:

Iron (Fe) 30 atoms
Calcium (Ca) 2 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State (pdb code 3min). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State, PDB code: 3min:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 3min

Go back to Molybdenum Binding Sites List in 3min
Molybdenum binding site 1 out of 2 in the Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo496

b:19.1
occ:1.00
MO1 A:CFM496 0.0 19.1 1.0
O7 A:HCA494 2.0 17.0 1.0
O5 A:HCA494 2.0 16.8 1.0
ND1 A:HIS442 2.1 17.8 1.0
S4B A:CFM496 2.2 18.8 1.0
S1B A:CFM496 2.2 16.8 1.0
S3B A:CFM496 2.3 18.1 1.0
FE7 A:CFM496 2.6 16.2 1.0
FE6 A:CFM496 2.6 19.8 1.0
FE5 A:CFM496 2.7 17.7 1.0
C7 A:HCA494 3.0 19.7 1.0
CE1 A:HIS442 3.0 14.6 1.0
C3 A:HCA494 3.1 20.2 1.0
CG A:HIS442 3.2 14.9 1.0
CB A:HIS442 3.8 16.0 1.0
C2 A:HCA494 4.1 21.8 1.0
NE2 A:HIS442 4.1 14.7 1.0
O6 A:HCA494 4.2 17.9 1.0
C4 A:HCA494 4.2 19.6 1.0
O A:HOH530 4.2 14.7 1.0
CD2 A:HIS442 4.3 11.0 1.0
CA A:HIS442 4.6 18.8 1.0
O1 A:HCA494 4.6 24.7 1.0
S3A A:CFM496 4.7 17.1 1.0
S5 A:CFM496 4.7 15.1 1.0
S2B A:CFM496 4.7 18.4 1.0
C1 A:HCA494 4.8 23.3 1.0
FE2 A:CFM496 4.9 17.7 1.0
FE3 A:CFM496 5.0 19.3 1.0

Molybdenum binding site 2 out of 2 in 3min

Go back to Molybdenum Binding Sites List in 3min
Molybdenum binding site 2 out of 2 in the Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Mofe Protein From Azotobacter Vinelandii, Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo496

b:20.8
occ:1.00
MO1 C:CFM496 0.0 20.8 1.0
O7 C:HCA494 2.1 17.7 1.0
O5 C:HCA494 2.1 20.0 1.0
ND1 C:HIS442 2.2 17.9 1.0
S3B C:CFM496 2.2 19.4 1.0
S1B C:CFM496 2.2 20.9 1.0
S4B C:CFM496 2.3 20.9 1.0
FE6 C:CFM496 2.6 19.6 1.0
FE7 C:CFM496 2.7 21.3 1.0
FE5 C:CFM496 2.7 20.6 1.0
CE1 C:HIS442 3.0 20.3 1.0
C7 C:HCA494 3.0 20.1 1.0
C3 C:HCA494 3.1 17.9 1.0
CG C:HIS442 3.2 17.4 1.0
CB C:HIS442 3.8 18.0 1.0
C2 C:HCA494 4.0 18.3 1.0
NE2 C:HIS442 4.2 18.2 1.0
O C:HOH534 4.2 30.8 1.0
O6 C:HCA494 4.2 17.0 1.0
C4 C:HCA494 4.2 17.5 1.0
CD2 C:HIS442 4.3 17.5 1.0
C5 C:HCA494 4.4 13.3 1.0
O2 C:HCA494 4.5 19.4 1.0
S5 C:CFM496 4.6 23.6 1.0
CA C:HIS442 4.6 19.4 1.0
S2B C:CFM496 4.7 21.0 1.0
S3A C:CFM496 4.8 19.4 1.0
C1 C:HCA494 4.8 16.2 1.0
FE3 C:CFM496 4.9 23.4 1.0
FE4 C:CFM496 5.0 21.6 1.0

Reference:

J.W.Peters, M.H.Stowell, S.M.Soltis, M.G.Finnegan, M.K.Johnson, D.C.Rees. Redox-Dependent Structural Changes in the Nitrogenase P-Cluster. Biochemistry V. 36 1181 1997.
ISSN: ISSN 0006-2960
PubMed: 9063865
DOI: 10.1021/BI9626665
Page generated: Tue Dec 15 05:18:11 2020

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