› 1h16

X-ray diffraction
1.53Å resolution

Pyruvate Formate-Lyase (E.coli) in complex with Pyruvate and CoA

Released:
DOI: 10.2210/pdb1h16/pdb
PDB entry 1h16 coloured by chain, front view.
PDB entry 1h16 coloured by chain, side view.
PDB entry 1h16 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 PYR 1 x PYR
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: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: C2221
Unit cell:
a: 54.9Å b: 153.05Å c: 205.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.145 0.163

Quick links

Citations

11 review citations

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

10 mentions without citation

The origin and evolution of ribonucleotide reduction.
Lundin et al. (2015)
9 more