Research workbench
Methane monooxygenase hydroxylase
Analyse Methane monooxygenase hydroxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MHZ
- Type
- protein
- Length
- 1,060 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methane monooxygenase hydroxylase
- EC
- 1.14.13.25
- UniProt
- P27354, P27353, P27355
- Ligands
- FE
- Pockets
- 11 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Methane monooxygenase hydroxylase (EC 1.14.13.25) | protein | 383 | 66% helix, 1% strand | P27354 |
| D | Methane monooxygenase hydroxylase (EC 1.14.13.25) | protein | 510 | 63% helix, 4% strand | P27353 |
| G | Methane monooxygenase hydroxylase (EC 1.14.13.25) | protein | 167 | 64% helix, 4% strand | P27355 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.81 | 0.97 | 32 | empty |
| 2 | 117 | 0.80 | 0.98 | 26 | empty |
| 3 | 117 | 0.72 | 0.93 | 28 | empty |
| 4 | 225 | 0.53 | 0.77 | 30 | empty |
| 5 | 116 | 0.48 | 0.80 | 19 | empty |
Interfaces
3 interfaces between chains.
- B–D · 5164 Ų buried · 83 hydrogen bonds · protein-protein
- D–G · 2171 Ų buried · 38 hydrogen bonds · protein-protein
- B–G · 1366 Ų buried · 21 hydrogen bonds · protein-protein
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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