› 2wpn

X-ray diffraction
2.04Å resolution

Function and Biology Details

Reactions catalysed: 
H(2) + 2 ferricytochrome c3 = 2 H(+) + 2 ferrocytochrome c3
H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180786 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cytochrome-c3 hydrogenase Chain: A
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 33.94 KDa
Source organism: Nitratidesulfovibrio vulgaris str. Hildenborough
UniProt:
  • Canonical: Q72AS4 (Residues: 1-317; Coverage: 100%)
Gene names: DVU_1917, hysB
Sequence domains:
Structure domains:
Periplasmic [NiFeSe] hydrogenase, large subunit, selenocysteine-containing Chain: B
Molecule details ›
Chain: B
Length: 495 amino acids
Theoretical weight: 54.45 KDa
Source organism: Nitratidesulfovibrio vulgaris str. Hildenborough
UniProt:
  • Canonical: Q72AS3 (Residues: 1-495; Coverage: 97%)
Gene names: DVU_1918, hysA
Sequence domains: Nickel-dependent hydrogenase
Structure domains: Cytochrome-c3 Hydrogenase, chain B

Ligands and Environments

7 bound ligands:
Ligand SF4 3 x SF4
Ligand FSX 1 x FSX
Ligand SBY 4 x SBY
Ligand FCO 1 x FCO
Ligand NI 1 x NI
Ligand FE2 1 x FE2
Ligand CL 1 x CL
2 modified residues:
Ligand OCS 1 x OCS
Ligand PSW 1 x PSW

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 60.596Å b: 91.223Å c: 66.751Å
α: 90° β: 101.73° γ: 90°
R-values:
R R work R free
0.147 0.144 0.201

Quick links

Citations

9 review citations

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
8 more

8 mentions without citation

Molecular regulation of conditioning film formation and quorum quenching in sulfate reducing bacteria.
Raya et al. (2022)
7 more