› 1qhm

X-ray diffraction
2.8Å resolution

ESCHERICHIA COLI PYRUVATE FORMATE LYASE LARGE DOMAIN

Released:
DOI: 10.2210/pdb1qhm/pdb
PDB entry 1qhm coloured by chain, front view.
PDB entry 1qhm coloured by chain, side view.
PDB entry 1qhm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase.
Leppänen VM, Merckel MC, Ollis DL, Wong KK, Kozarich JW, Goldman A
Structure 7 733-44 (1999)
PMID: 10425676

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + formate = CoA + pyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formate acetyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 624 amino acids
Theoretical weight: 70.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09373 (Residues: 2-625; Coverage: 82%)
Gene names: JW0886, b0903, pfl, pflB
Sequence domains: Pyruvate formate lyase-like
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P65
Unit cell:
a: 140.8Å b: 140.8Å c: 215.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.228 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
8 more