2cqy

Solution NMR

Solution structure of B domain from human propionyl-CoA carboxylase alpha subunit

Released:
Source organism: Homo sapiens
Entry authors: Suetake T, Hayashi F, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-138576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Propionyl-CoA carboxylase alpha chain, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 11.41 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05165 (Residues: 176-270; Coverage: 13%)
Gene name: PCCA
Sequence domains: Carbamoyl-phosphate synthase L chain, ATP binding domain
Structure domains: ATP-grasp fold, A domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Not provided