PDBe 1jc5

X-ray diffraction
2.2Å resolution

Crystal Structure of Native Methylmalonyl-CoA Epimerase

Released:

Function and Biology Details

Reaction catalysed:
(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylmalonyl CoA epimerase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 148 amino acids
Theoretical weight: 16.74 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8VQN0 (Residues: 1-148; Coverage: 100%)
Gene names: PFREUDJS001_001024, epi
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 55.985Å b: 114.02Å c: 156.418Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.248 0.293
Expression system: Escherichia coli BL21