› 2xiq

X-ray diffraction
1.95Å resolution

Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin and malonyl-CoA

Released:
DOI: 10.2210/pdb2xiq/pdb
PDB entry 2xiq coloured by chain, front view.
PDB entry 2xiq coloured by chain, side view.
PDB entry 2xiq 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 BL21(DE3)
UniProt:
  • Canonical: P22033 (Residues: 12-750; Coverage: 99%)
Gene names: MMUT, MUT
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand B12 2 x B12
2 bound ligands:
Ligand 5AD 2 x 5AD
Ligand MLC 2 x MLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 75.65Å b: 143.62Å c: 163.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

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

10 mentions without citation

Structural diversity in the AdoMet radical enzyme superfamily.
Dowling et al. (2012)
9 more