› 3f46

X-ray diffraction
1.95Å resolution

The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme from Methanocaldococcus jannaschii

Released:
DOI: 10.2210/pdb3f46/pdb
PDB entry 3f46 coloured by chain, front view.
PDB entry 3f46 coloured by chain, side view.
PDB entry 3f46 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex.
Hiromoto T, Ataka K, Pilak O, Vogt S, Stagni MS, Meyer-Klaucke W, Warkentin E, Thauer RK, Shima S, Ermler U
FEBS Lett 583 585-90 (2009)
PMID: 19162018

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-176577 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5,10-methenyltetrahydromethanopterin hydrogenase Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 38.71 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58194 (Residues: 1-358; Coverage: 100%)
Gene names: MJ0784, hmd
Sequence domains: H2-forming N5,N10-methylene-tetrahydromethanopterin dehydrogenase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand I2C 1 x I2C
Ligand FE2 1 x FE2
Ligand CMO 2 x CMO
Ligand DTV 1 x DTV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: I4122
Unit cell:
a: 96.35Å b: 96.35Å c: 166.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.165 0.205
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Radical S-adenosylmethionine enzymes.
Broderick et al. (2014)
15 more