› 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:
DOI: 10.2210/pdb2jku/pdb
PDB entry 2jku coloured by chain, front view.
PDB entry 2jku coloured by chain, side view.
PDB entry 2jku coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural impact of human and Escherichia coli biotin carboxyl carrier proteins on biotin attachment.
Healy S, McDonald MK, Wu X, Yue WW, Kochan G, Oppermann U, Gravel RA
Biochemistry 49 4687-94 (2010)
PMID: 20443544

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138577 (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%)
Gene name: PCCA
Sequence domains: Biotin-requiring enzyme

Ligands and Environments

1 bound ligand:
Ligand PG4 2 x PG4
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)

Quick links

Citations

3 review citations

Structure and function of biotin-dependent carboxylases.
Tong L. (2013)
2 more

10 mentions without citation

From structural biology to designing therapy for inborn errors of metabolism.
Yue WW. (2016)
9 more