4gwb

X-ray diffraction
1.2Å resolution

Crystal structure of putative Peptide methionine sulfoxide reductase from Sinorhizobium meliloti 1021

Released:
Source organism: Sinorhizobium meliloti 1021
Entry authors: Malashkevich VN, Bhosle R, Toro R, Hillerich B, Gizzi A, Garforth S, Kar A, Chan MK, Lafluer J, Patel H, Matikainen B, Chamala S, Lim S, Celikgil A, Villegas G, Evans B, Zenchek W, Love J, Fiser A, Khafizov K, Seidel R, Bonanno JB, Almo SC, New York Structural Genomics Research Consortium (NYSGRC)

Function and Biology Details

Reaction catalysed:
L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide methionine sulfoxide reductase MsrA 3 Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 19.46 KDa
Source organism: Sinorhizobium meliloti 1021
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92Y45 (Residues: 1-168; Coverage: 100%)
Gene names: RA1043, SMa1896, msrA3
Sequence domains: Peptide methionine sulfoxide reductase
Structure domains: Peptide methionine sulphoxide reductase MsrA

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2221
Unit cell:
a: 44.778Å b: 72.151Å c: 97.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.18
Expression system: Escherichia coli BL21(DE3)