› 6gm6

X-ray diffraction
1.61Å resolution

[FeFe]-hydrogenase HydA1 from Chlamydomonas reinhardtii,variant E141Q

Released:
DOI: 10.2210/pdb6gm6/pdb
PDB entry 6gm6 coloured by chain, front view.
PDB entry 6gm6 coloured by chain, side view.
PDB entry 6gm6 coloured by chain, top view.
Source organism: Chlamydomonas reinhardtii
Primary publication:
Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases.
Duan J, Senger M, Esselborn J, Engelbrecht V, Wittkamp F, Apfel UP, Hofmann E, Stripp ST, Happe T, Winkler M
OpenAccess logo Nat Commun 9 4726 (2018)
PMID: 30413719

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: 48.88 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

3 bound ligands:
Ligand SF4 1 x SF4
Ligand CL 1 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 70.79Å b: 70.79Å c: 155.03Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.164 0.199
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

A personal account on 25 years of scientific literature on [FeFe]-hydrogenase.
Sidabras et al. (2023)
1 more

1 mention without citation

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