› 2gvi

X-ray diffraction
1.87Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-190848 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formylmethanofuran dehydrogenase subunit E domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 204 amino acids
Theoretical weight: 23.45 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HJ63 (Residues: 1-203; Coverage: 100%)
Gene name: Ta1109
Sequence domains: FmdE, Molybdenum formylmethanofuran dehydrogenase operon
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 5 x ZN
Ligand UNL 1 x UNL
Ligand EDO 6 x EDO
Ligand ACY 8 x ACY
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1, SSRL BEAMLINE BL9-2
Spacegroup: I222
Unit cell:
a: 78.68Å b: 97.65Å c: 75.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.217
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Biochemical fossils of the ancient transition from geoenergetics to bioenergetics in prokaryotic one carbon compound metabolism.
Sousa et al. (2014)
3 more

2 mentions without citation

Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved α+β core domain and an auxiliary C-terminal treble-clef zinc finger.
Axelrod et al. (2010)
1 more