6op4

X-ray diffraction
2.3Å resolution

Selenium-incorporated, carbon monoxide-inhibited, reactivated FeMo-cofactor of nitrogenase from Azotobacter vinelandii

Released:

Function and Biology Details

Reaction catalysed:
8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nitrogenase molybdenum-iron protein alpha chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 477 amino acids
Theoretical weight: 54 KDa
Source organism: Azotobacter vinelandii
UniProt:
  • Canonical: P07328 (Residues: 4-480; Coverage: 97%)
Gene name: nifD
Sequence domains: Nitrogenase component 1 type Oxidoreductase
Nitrogenase molybdenum-iron protein beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 522 amino acids
Theoretical weight: 59.4 KDa
Source organism: Azotobacter vinelandii
UniProt:
  • Canonical: P07329 (Residues: 2-523; Coverage: 100%)
Gene name: nifK
Sequence domains: Nitrogenase component 1 type Oxidoreductase

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 76.981Å b: 129.326Å c: 106.755Å
α: 90° β: 108.84° γ: 90°
R-values:
R R work R free
0.178 0.176 0.223