› 8xl8

Electron Microscopy
2.36Å resolution

Structure of human 3-methylcrotonyl-CoA carboxylase in complex with propionyl-CoA (MCC-PCO)

Released:
DOI: 10.2210/pdb8xl8/pdb
PDB entry 8xl8 coloured by chain, front view.
PDB entry 8xl8 coloured by chain, side view.
PDB entry 8xl8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into human propionyl-CoA carboxylase (PCC) and 3-methylcrotonyl-CoA carboxylase (MCC)
Zhou F, Zhang Y, Zhu Y, Zhou Q, Shi Y, Hu Q
Elife (2024)
Related structures: EMD-38441

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:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-275276 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 725 amino acids
Theoretical weight: 80.58 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q96RQ3 (Residues: 1-725; Coverage: 100%)
Gene names: MCCA, MCCC1
Sequence domains:
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 563 amino acids
Theoretical weight: 61.41 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q9HCC0 (Residues: 1-563; Coverage: 100%)
Gene names: MCCB, MCCC2
Sequence domains: Carboxyl transferase domain

Ligands and Environments


Cofactor: Ligand BTN 6 x BTN
1 bound ligand:
Ligand 1VU 6 x 1VU
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.36Å
Relevant EMDB volumes: EMD-38441

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