› 7wtc

Electron Microscopy
4Å resolution

Cryo-EM structure of human pyruvate carboxylase with acetyl-CoA in the ground state

Released:
DOI: 10.2210/pdb7wtc/pdb
PDB entry 7wtc coloured by chain, front view.
PDB entry 7wtc coloured by chain, side view.
PDB entry 7wtc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA.
Chai P, Lan P, Li S, Yao D, Chang C, Cao M, Shen Y, Ge S, Wu J, Lei M, Fan X
Mol Cell (2022)
PMID: 36283412
Related structures: EMD-32778

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145858 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate carboxylase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1178 amino acids
Theoretical weight: 129.8 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P11498 (Residues: 1-1178; Coverage: 100%)
Gene name: PC
Sequence domains:

Ligands and Environments


Cofactor: Ligand BTI 4 x BTI
1 bound ligand:
Ligand ACO 2 x ACO
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4Å
Relevant EMDB volumes: EMD-32778

Quick links

Citations

1 citations in other articles

Allosteric Site at the Biotin Carboxylase Dimer Interface Mediates Activation and Inhibition in Staphylococcus aureus Pyruvate Carboxylase.
Laseke et al. (2023)