MolNFT v1 · #14697 · protein
Methane monooxygenase hydroxylase
1MHZ: “Methane monooxygenase hydroxylase”. X-ray diffraction. MolNFT v1 #14697 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MHZ
- Type
- protein
- Length
- 1,060 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P27354, P27353, P27355
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 383 | — | P27354 |
| D | — | protein | 510 | — | P27353 |
| G | — | protein | 167 | — | P27355 |
Compared structures
- 1MHZ · Methane monooxygenase hydroxylase · the same entry in another collection · chain B against B, TM-score 1.00
- P27353 · 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
- P27355 · 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 0.99
- P27354 · 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 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P27354
- Every structure of UniProt P27353
- Every structure of UniProt P27355
- Elsewhere: RCSB PDB 1MHZ · PDBe 1MHZ · UniProt P27354 · UniProt P27353 · UniProt P27355
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