X-ray diffraction
2.12Å resolution

Crystal structure of pyruvate oxidoreductase subunit PORC (EC (TM0015) from Thermotoga maritima at 2.12 A resolution

Source organism: Thermotoga maritima MSB8
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reaction catalysed:
Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Pyruvate synthase subunit PorC Chain: A
Molecule details ›
Chain: A
Length: 204 amino acids
Theoretical weight: 23.04 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
  • Canonical: O05650 (Residues: 1-192; Coverage: 100%)
Gene names: TM_0015, porC, porG
Sequence domains: Pyruvate ferredoxin/flavodoxin oxidoreductase
Structure domains: Pyruvate-ferredoxin oxidoreductase, PFOR, domain III

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2, SSRL BEAMLINE BL11-1
Spacegroup: P41212
Unit cell:
a: 57.252Å b: 57.252Å c: 147.151Å
α: 90° β: 90° γ: 90°
R R work R free
0.217 0.215 0.251
Expression system: Escherichia coli