› 3bic

X-ray diffraction
2.6Å resolution

Crystal structure of human methylmalonyl-CoA mutase

Released:
DOI: 10.2210/pdb3bic/pdb
PDB entry 3bic coloured by chain, front view.
PDB entry 3bic coloured by chain, side view.
PDB entry 3bic coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation.
Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW
J Biol Chem 285 38204-13 (2010)
PMID: 20876572

Function and Biology Details

Reaction catalysed: 
(R)-methylmalonyl-CoA = succinyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-149507 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylmalonyl-CoA mutase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 762 amino acids
Theoretical weight: 84.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22033 (Residues: 12-750; Coverage: 99%)
Gene names: MMUT, MUT
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 103.75Å b: 95.15Å c: 119.16Å
α: 90° β: 108.31° γ: 90°
R-values:
R R work R free
0.218 0.217 0.243
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Vitamin B12-derivatives-enzyme cofactors and ligands of proteins and nucleic acids.
Gruber et al. (2011)
13 more

5 mentions without citation

Genetic disorders of vitamin B₁₂ metabolism: eight complementation groups--eight genes.
Froese et al. (2010)
4 more