› 6nac

X-ray diffraction
1.55Å resolution

Crystal structure of [FeFe]-hydrogenase I (CpI) solved with single pulse free electron laser data

Released:
DOI: 10.2210/pdb6nac/pdb
PDB entry 6nac coloured by chain, front view.
PDB entry 6nac coloured by chain, side view.
PDB entry 6nac coloured by chain, top view.
Source organism: Clostridium pasteurianum
Primary publication:
Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases.
Artz JH, Zadvornyy OA, Mulder DW, Keable SM, Cohen AE, Ratzloff MW, Williams SG, Ginovska B, Kumar N, Song J, McPhillips SE, Davidson CM, Lyubimov AY, Pence N, Schut GJ, Jones AK, Soltis SM, Adams MWW, Raugei S, King PW, Peters JW
J Am Chem Soc 142 1227-1235 (2020)
PMID: 31816235

Function and Biology Details

Reaction catalysed: 
H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Iron hydrogenase 1 Chain: A
Molecule details ›
Chain: A
Length: 574 amino acids
Theoretical weight: 63.91 KDa
Source organism: Clostridium pasteurianum
Expression system: Clostridium pasteurianum
UniProt:
  • Canonical: P29166 (Residues: 1-574; Coverage: 100%)
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand 402 1 x 402
Ligand SF4 4 x SF4
Ligand FES 1 x FES
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLAC LCLS BEAMLINE XPP
Spacegroup: P42212
Unit cell:
a: 111.165Å b: 111.165Å c: 104.007Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.285
Expression system: Clostridium pasteurianum

Quick links

Citations

5 review citations

Fantastic [FeFe]-Hydrogenases and Where to Find Them.
Morra S. (2022)
4 more

3 mentions without citation

Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.
Stripp et al. (2022)
2 more