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X-ray diffraction
2.64Å resolution

Crystal Structure of Methylmalonic Acidemia Type A Protein

Released:
DOI: 10.2210/pdb2www/pdb
PDB entry 2www coloured by chain, front view.
PDB entry 2www coloured by chain, side view.
PDB entry 2www 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

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184871 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylmalonic aciduria type A protein, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 349 amino acids
Theoretical weight: 38.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8IVH4 (Residues: 70-418; Coverage: 84%)
Gene name: MMAA
Sequence domains: Methylmalonyl Co-A mutase-associated GTPase MeaB
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 2PE 3 x 2PE
Ligand GDP 4 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P42
Unit cell:
a: 149.43Å b: 149.43Å c: 69.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.222
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

17 mentions without citation

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