2afr

X-ray diffraction
2.3Å resolution

The Crystal Structure of Putative Precorrin Isomerase CbiC in Cobalamin Biosynthesis

Released:
Source organism: Leptospira interrogans
Primary publication:
The crystal structure of putative precorrin isomerase CbiC in cobalamin biosynthesis.
J Struct Biol 153 307-11 (2006)
PMID: 16427313

Function and Biology Details

Reaction catalysed:
Cobalt-precorrin-8 = cobyrinate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-184435 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cobalt-precorrin-8 methylmutase Chain: A
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 25.89 KDa
Source organism: Leptospira interrogans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EXP7 (Residues: 1-220; Coverage: 100%)
Gene names: LB_161, cbiC
Sequence domains: Precorrin-8X methylmutase
Structure domains: Cobalamin biosynthesis CobH/CbiC, precorrin-8X methylmutase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P3121
Unit cell:
a: 55.885Å b: 55.885Å c: 142.551Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.224 0.284
Expression system: Escherichia coli