3cez

X-ray diffraction
2.1Å resolution

Crystal structure of methionine-R-sulfoxide reductase from Burkholderia pseudomallei

Released:
Entry authors: Staker B, Napuli A, Nakazawa SH, Castaneda L, Alkafeef S, Vanvoorhis W, Stewart L, Myler P, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-174667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide methionine sulfoxide reductase MsrB Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.5 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3JRF0 (Residues: 1-143; Coverage: 100%)
Gene names: BURPS1710b_2458, msrB
Sequence domains: SelR domain
Structure domains: Peptide methionine sulfoxide reductase.

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 42.093Å b: 45.782Å c: 45.812Å
α: 87.35° β: 83.22° γ: 69.36°
R-values:
R R work R free
0.179 0.176 0.234
Expression system: Escherichia coli