PDBe 2idx

X-ray diffraction
2.5Å resolution

Structure of Human ATP:Cobalamin adenosyltransferase bound to ATP.

Released:
Source organism: Homo sapiens
Primary publication:
Structure of ATP-bound human ATP:cobalamin adenosyltransferase.
Biochemistry 45 15188-96 (2006)
PMID: 17176040

Function and Biology Details

Reaction catalysed:
(1) ATP + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide. (2) ATP + cobinamide = triphosphate + adenosylcobinamide. 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 196 amino acids
Theoretical weight: 21.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96EY8 (Residues: 56-250; Coverage: 78%)
Gene name: MMAB
Sequence domains: Cobalamin adenosyltransferase
Structure domains: Hypothetical Protein Ta1238; Chain: A;

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P3121
Unit cell:
a: 111.238Å b: 111.238Å c: 115.526Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.197 0.251
Expression system: Escherichia coli