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Methane monooxygenase hydroxylase from methylococcus capsulatus (bath)

Analyse Methane monooxygenase hydroxylase from methylococcus capsulatus (bath) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MTY
Type
protein
Length
2,116 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P22869, P18798, P11987

Structure

x-ray diffraction · 3 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
D, E—protein512—P22869
B, C—protein384—P18798
G, H—protein162—P11987

Compared structures

  • 1MTY · Methane monooxygenase hydroxylase from methylococcus capsulatus (bath) · the same entry in another collection · chain H against H, TM-score 1.00
  • P18798 · AlphaFold monomer V2.0 prediction for methane monooxygenase component a beta chain… · a predicted model of the same protein · chain B against A, TM-score 1.00
  • P11987 · AlphaFold monomer V2.0 prediction for methane monooxygenase component a gamma chain… · a predicted model of the same protein · chain G against A, TM-score 1.00
  • P22869 · AlphaFold monomer V2.0 prediction for methane monooxygenase component a alpha chain… · a predicted model of the same protein · chain D against A, TM-score 1.00

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