2jku

X-ray diffraction
1.5Å resolution

Crystal structure of the N-terminal region of the biotin acceptor domain of human propionyl-CoA carboxylase

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Propionyl-CoA carboxylase alpha chain, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 94 amino acids
Theoretical weight: 9.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05165 (Residues: 658-728; Coverage: 10%)
  • Best match: P05165-3 (Residues: 631-681)
Gene name: PCCA
Sequence domains: Biotin-requiring enzyme

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P6422
Unit cell:
a: 56.107Å b: 56.107Å c: 58.083Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.148 0.166
Expression system: Escherichia coli BL21(DE3)