Research workbench
Complex structure of methane monooxygenase hydroxylase and regulatory subunit
Analyse Complex structure of methane monooxygenase hydroxylase and regulatory subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GAM
- Type
- protein
- Length
- 4,788 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methane monooxygenase component a beta chain; Methane monooxygenase component a alpha…
- EC
- 1.14.13.25
- UniProt
- P18798, P22869, P11987, P18797
- Ligands
- FE
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 4 distinct chains · 56% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, G, L, Q | Methane monooxygenase component a beta chain (EC 1.14.13.25) | protein | 388 | 61% helix, 1% strand | P18798 |
| A, F, K, P | Methane monooxygenase component a alpha chain (EC 1.14.13.25) | protein | 511 | 57% helix, 4% strand | P22869 |
| C, H, M, R | Methane monooxygenase component a gamma chain (EC 1.14.13.25) | protein | 166 | 61% helix, 4% strand | P11987 |
| D, I, N, S | Methane monooxygenase regulatory protein B | protein | 132 | 31% helix, 28% strand | P18797 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 8 copies · chains A, F, K, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1034 | 0.88 | 0.90 | 111 | empty |
| 2 | 1000 | 0.88 | 0.89 | 101 | empty |
| 3 | 1010 | 0.84 | 0.85 | 100 | empty |
| 4 | 1170 | 0.82 | 0.83 | 106 | empty |
| 5 | 80 | 0.77 | 0.99 | 33 | empty |
Interfaces
43 interfaces between chains.
- B–A · 5256 Ų buried · 80 hydrogen bonds · protein-protein
- L–K · 5247 Ų buried · 84 hydrogen bonds · protein-protein
- G–F · 5242 Ų buried · 78 hydrogen bonds · protein-protein
- Q–P · 5222 Ų buried · 69 hydrogen bonds · protein-protein
- P–S · 2734 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 4GAM · Complex structure of Methane monooxygenase hydroxylase and regulatory subunit · the same entry in another collection · chain S against S, TM-score 1.00
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 P18798
- Every structure of UniProt P22869
- Every structure of UniProt P11987
- Every structure of UniProt P18797
- Elsewhere: RCSB PDB 4GAM · PDBe 4GAM · UniProt P18798 · UniProt P22869 · UniProt P11987 · UniProt P18797
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