2ejm

Solution NMR

Solution structure of RUH-072, an apo-biotnyl domain form human acetyl coenzyme A carboxylase

Released:
Source organism: Homo sapiens
Entry authors: Ruhul Momen AZM, Hirota H, Hayashi F, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188732 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96RQ3 (Residues: 640-725; Coverage: 12%)
Gene names: MCCA, MCCC1
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli