› 3wv7

X-ray diffraction
1.6Å resolution

HcgE from Methanothermobacter marburgensis

Released:
DOI: 10.2210/pdb3wv7/pdb
PDB entry 3wv7 coloured by chain, front view.
PDB entry 3wv7 coloured by chain, side view.
PDB entry 3wv7 coloured by chain, top view.
Source organism: Methanothermobacter marburgensis str. Marburg
Primary publication:
Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor.
Fujishiro T, Kahnt J, Ermler U, Shima S
Nat Commun 6 6895 (2015)
PMID: 25882909

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
THIF-type NAD/FAD binding fold domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 218 amino acids
Theoretical weight: 23.74 KDa
Source organism: Methanothermobacter marburgensis str. Marburg
Expression system: Escherichia coli
UniProt:
  • Canonical: D9PY12 (Residues: 1-212; Coverage: 100%)
Gene names: MTBMA_c15310, hcgE
Sequence domains: ThiF family

Ligands and Environments

1 bound ligand:
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 68.39Å b: 73.52Å c: 68.58Å
α: 90° β: 118.05° γ: 90°
R-values:
R R work R free
0.167 0.165 0.199
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.
Schilter et al. (2016)
2 more