› 1cm5

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF C418A,C419A MUTANT OF PFL FROM E.COLI

Released:
DOI: 10.2210/pdb1cm5/pdb
PDB entry 1cm5 coloured by chain, front view.
PDB entry 1cm5 coloured by chain, side view.
PDB entry 1cm5 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase.
Becker A, Fritz-Wolf K, Kabsch W, Knappe J, Schultz S, Volker Wagner AF
Nat Struct Biol 6 969-75 (1999)
PMID: 10504733

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: 759 amino acids
Theoretical weight: 85.26 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

2 bound ligands:
Ligand CO3 2 x CO3
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P43212
Unit cell:
a: 159.059Å b: 159.059Å c: 159.784Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.251

Quick links

Citations

26 review citations

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

2 mentions without citation

Structural modeling of protein interactions by analogy: application to PSD-95.
Korkin et al. (2006)
1 more