X-ray diffraction
3.35Å resolution

Isobutyryl-CoA mutase fused with bound adenosylcobalamin, GDP, and Mg (holo-IcmF/GDP)

Primary publication:
Visualization of a radical B12 enzyme with its G-protein chaperone.
Proc Natl Acad Sci U S A 112 2419-24 (2015)
PMID: 25675500

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-172959 (preferred)
Entry contents:
1 distinct polypeptide molecule
Fused isobutyryl-CoA mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 1113 amino acids
Theoretical weight: 122.93 KDa
Source organism: Cupriavidus metallidurans CH34
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q1LRY0 (Residues: 1-1093; Coverage: 100%)
Gene names: Rmet_0210, icmF, sbm
Sequence domains:

Ligands and Environments

Cofactor: Ligand B12 2 x B12
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: R32
Unit cell:
a: 318.76Å b: 318.76Å c: 343.52Å
α: 90° β: 90° γ: 120°
R R work R free
0.181 0.18 0.198
Expression system: Escherichia coli BL21(DE3)