› 3rgb

X-ray diffraction
2.8Å resolution

Crystal structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath)

Released:
DOI: 10.2210/pdb3rgb/pdb
PDB entry 3rgb coloured by chain, front view.
PDB entry 3rgb coloured by chain, side view.
PDB entry 3rgb coloured by chain, top view.
Source organism: Methylococcus capsulatus
Primary publication:
Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M.
Smith SM, Rawat S, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC
Biochemistry 50 10231-40 (2011)
PMID: 22013879

Function and Biology Details

Reactions catalysed: 
Methane + quinol + O(2) = methanol + quinone + H(2)O
Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
PDBe Complex ID:
PDB-CPX-124232 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Particulate methane monooxygenase alpha subunit Chains: A, E, I
Molecule details ›
Chains: A, E, I
Length: 414 amino acids
Theoretical weight: 46.13 KDa
Source organism: Methylococcus capsulatus
UniProt:
  • Canonical: G1UBD1 (Residues: 1-414; Coverage: 100%)
Gene names: MCA1796, MCA2853, pmoB, pmoB1, pmoB2
Sequence domains: Monooxygenase subunit B protein
Structure domains:
Particulate methane monooxygenase beta subunit Chains: B, F, J
Molecule details ›
Chains: B, F, J
Length: 247 amino acids
Theoretical weight: 28.45 KDa
Source organism: Methylococcus capsulatus
UniProt:
  • Canonical: Q607G3 (Residues: 1-247; Coverage: 100%)
Gene names: MCA1797, MCA2854, pmoA, pmoA1, pmoA2
Sequence domains: Ammonia monooxygenase
Structure domains: Ammonia/particulate methane monooxygenase, subunit A
Methane monooxygenase, C subunit Chains: C, G, K
Molecule details ›
Chains: C, G, K
Length: 289 amino acids
Theoretical weight: 33.21 KDa
Source organism: Methylococcus capsulatus
UniProt:
  • Canonical: Q603F1 (Residues: 1-260; Coverage: 100%)
Gene names: MCA1798, MCA2855, pmoC1
Sequence domains: Ammonia monooxygenase/methane monooxygenase, subunit C
Structure domains: Particulate methane monooxygenase subunit c2. Chain: C

Ligands and Environments

3 bound ligands:
Ligand CU 3 x CU
Ligand ZN 9 x ZN
Ligand CUA 3 x CUA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P42212
Unit cell:
a: 264.14Å b: 264.14Å c: 150.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.27 0.269 0.296

Quick links

Citations

11 review citations

Copper active sites in biology.
Solomon et al. (2014)
10 more

19 mentions without citation

Enzymatic oxidation of methane.
Sirajuddin et al. (2015)
18 more