9cl5

Electron Microscopy
2.48Å resolution

particulate methane monooxygenase in native membranes

Released:
Source organism: Methylocystis sp. ATCC 49242
Primary publication:
Structures of methane and ammonia monooxygenases in native membranes.
Proc Natl Acad Sci U S A 122 e2417993121 (2025)
PMID: 39739801
Related structures: EMD-45662

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-286376 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Methane monooxygenase/ammonia monooxygenase subunit A Chains: Ba, Bb, Bc
Molecule details ›
Chains: Ba, Bb, Bc
Length: 244 amino acids
Theoretical weight: 27.8 KDa
Source organism: Methylocystis sp. ATCC 49242
UniProt:
  • Canonical: A0A5R8QJU8 (Residues: 9-252; Coverage: 97%)
Gene name: FEV16_06660
Sequence domains: Ammonia monooxygenase
Methane monooxygenase/ammonia monooxygenase subunit B Chains: Aa, Ab, Ac
Molecule details ›
Chains: Aa, Ab, Ac
Length: 388 amino acids
Theoretical weight: 42.79 KDa
Source organism: Methylocystis sp. ATCC 49242
UniProt:
  • Canonical: A0A431PQN7 (Residues: 29-353, 355-415; Coverage: 99%)
Gene name: EKK29_10460
Sequence domains: Monooxygenase subunit B protein
Particulate methane monooxygenase subunit C Chains: Ca, Cb, Cc
particulate methane monooxygenase supernumerary helix Chains: Da, Db, Dc

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.48Å
Relevant EMDB volumes: EMD-45662