› 6hac

X-ray diffraction
2.3Å resolution

Crystal structure of [Fe]-hydrogenase (Hmd) holoenzyme from Methanococcus aeolicus (open form)

Released:
DOI: 10.2210/pdb6hac/pdb
PDB entry 6hac coloured by chain, front view.
PDB entry 6hac coloured by chain, side view.
PDB entry 6hac coloured by chain, top view.
Source organism: Methanococcus aeolicus Nankai-3
Primary publication:
The atomic-resolution crystal structure of activated [Fe]-hydrogenase
Huang G, Wagner T, Wodrich MD, Ataka K, Bill E, Ermler U, Hu X, Shima S
Nat Catal (2019)

Function and Biology Details

Reaction catalysed: 
H(2) + 5,10-methenyltetrahydromethanopterin = H(+) + 5,10-methylenetetrahydromethanopterin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108125 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5,10-methenyltetrahydromethanopterin hydrogenase Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 36.78 KDa
Source organism: Methanococcus aeolicus Nankai-3
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A6UVT1 (Residues: 1-342; Coverage: 100%)
Gene names: Maeo_1025, hmd
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand FE9 1 x FE9
Ligand 1PE 1 x 1PE
Ligand GOL 2 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: I4122
Unit cell:
a: 136.985Å b: 136.985Å c: 117.317Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.192
Expression system: Escherichia coli BL21(DE3)

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