› 4xc6

X-ray diffraction
3.35Å resolution

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

Released:
DOI: 10.2210/pdb4xc6/pdb
PDB entry 4xc6 coloured by chain, front view.
PDB entry 4xc6 coloured by chain, side view.
PDB entry 4xc6 coloured by chain, top view.
Source organism: Cupriavidus metallidurans CH34
Primary publication:
Visualization of a radical B12 enzyme with its G-protein chaperone.
Jost M, Cracan V, Hubbard PA, Banerjee R, Drennan CL
Proc Natl Acad Sci U S A 112 2419-24 (2015)
PMID: 25675500

Function and Biology Details

Reaction catalysed: 
2-methylpropanoyl-CoA = butanoyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172959 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • Canonical: Q1LRY0 (Residues: 1-1093; Coverage: 100%)
Gene names: Rmet_0210, icmF, sbm
Sequence domains:

Ligands and Environments


Cofactor: Ligand B12 2 x B12
4 bound ligands:
Ligand 5AD 1 x 5AD
Ligand GDP 2 x GDP
Ligand MG 4 x MG
Ligand ACT 1 x ACT
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-values:
R R work R free
0.181 0.18 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Vitamin B12 in the spotlight again.
Bridwell-Rabb et al. (2017)
2 more

9 mentions without citation

Metallochaperones and metalloregulation in bacteria.
Capdevila et al. (2017)
8 more