PDBe 1ff3

X-ray diffraction
1.9Å resolution

STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI

Released:

Function and Biology Details

Reaction catalysed:
(1) Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (S)-S-oxide + thioredoxin. (2) L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S- oxide + thioredoxin. 
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
homo tetramer
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide methionine sulfoxide reductase MsrA Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 211 amino acids
Theoretical weight: 23.31 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A744 (Residues: 2-212; Coverage: 100%)
Gene names: JW4178, b4219, msrA, pms
Sequence domains: Peptide methionine sulfoxide reductase
Structure domains: Peptide methionine sulfoxide reductase

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P6522
Unit cell:
a: 102.5Å b: 102.5Å c: 292.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.218