› 6gl6

X-ray diffraction
1.8Å resolution

apo [FeFe]-hydrogenase HydA1 from Chlamydomonas reinhardtii, variant C377H

Released:
DOI: 10.2210/pdb6gl6/pdb
Model geometry
Fit model/data
PDB entry 6gl6 coloured by chain, front view.
PDB entry 6gl6 coloured by chain, side view.
PDB entry 6gl6 coloured by chain, top view.
Source organism: Chlamydomonas reinhardtii
Primary publication:
His-Ligation to the [4Fe-4S] Subcluster Tunes the Catalytic Bias of [FeFe] Hydrogenase.
Rodríguez-Maciá P, Kertess L, Burnik J, Birrell JA, Hofmann E, Lubitz W, Happe T, Rüdiger O
J Am Chem Soc 141 472-481 (2019)
PMID: 30545220

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Iron hydrogenase small subunit domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 452 amino acids
Theoretical weight: 48.91 KDa
Source organism: Chlamydomonas reinhardtii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9FYU1 (Residues: 57-497; Coverage: 89%)
Gene names: CHLRE_03g199800v5, hyd1, hydA, hydA1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SF4 1 x SF4
Ligand CL 1 x CL
Ligand NA 2 x NA
Ligand SO3 1 x SO3
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P3221
Unit cell:
a: 70.73Å b: 70.73Å c: 155.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.169 0.197
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Reversible catalysis.
Fourmond et al. (2021)
1 more

1 mention without citation

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