› 1h17

X-ray diffraction
1.75Å resolution

Pyruvate Formate-Lyase (E.coli) in complex with CoA and the substrate analog oxamate

Released:
DOI: 10.2210/pdb1h17/pdb
PDB entry 1h17 coloured by chain, front view.
PDB entry 1h17 coloured by chain, side view.
PDB entry 1h17 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage.
Becker A, Kabsch W
J Biol Chem 277 40036-42 (2002)
PMID: 12163496

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 Chain: A
Molecule details ›
Chain: A
Length: 759 amino acids
Theoretical weight: 85.33 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P09373 (Residues: 2-760; Coverage: 100%)
Gene names: JW0886, b0903, pfl, pflB
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments


Cofactor: Ligand COA 1 x COA
5 bound ligands:
Ligand OXM 1 x OXM
Ligand NA 7 x NA
Ligand MG 1 x MG
Ligand DTL 2 x DTL
Ligand PG4 3 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOT/ENRAF-NONIUS
Spacegroup: C2221
Unit cell:
a: 54.938Å b: 153.169Å c: 205.909Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.148 0.173

Quick links

Citations

12 review citations

Ribonucleotide reductases.
Nordlund et al. (2006)
11 more