MolNFT v1 · #181874 · protein
Complex structure of methane monooxygenase hydroxylase and regulatory subunit with fluorosubstituted tryptophans
7M8R: “Complex structure of methane monooxygenase hydroxylase and regulatory subunit with fluorosubstituted…”. X-ray diffraction, 4 ligands (BEZ, W6X, FE). MolNFT v1 #181874 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7M8R
- Type
- protein
- Length
- 2,416 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2D2D5X0, A0A2D2D5X7, A0A2D2D0T0, A0A2D2D0T8
- Ligands
- BEZ, W6X, FE, CL
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | — | protein | 515 | — | A0A2D2D5X0 |
| B, F | — | protein | 392 | — | A0A2D2D5X7 |
| C, G | — | protein | 168 | — | A0A2D2D0T0 |
| D | — | protein | 130 | — | A0A2D2D0T8 |
| H | — | protein | 136 | — | A0A2D2D0T8 |
Ligands and binding sites
- BEZ · Benzoic acid · ligand · 2 copies · chains A, E
- W6X · 1,1,1-tris(fluoranyl)propan-2-one · ligand · 2 copies · chains D, H
- FE · Fe (III) ion · metal · 4 copies · chains A, E
- CL · Chloride ion · ion · chains D
- EDO · 1,2-ethanediol · additive · 38 copies · chains A, D, B, C, H, F, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M8R · Complex structure of Methane monooxygenase hydroxylase and regulatory subunit with… · the same entry in another collection · chain A against A, 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 A0A2D2D5X0
- Every structure of UniProt A0A2D2D5X7
- Every structure of UniProt A0A2D2D0T0
- Every structure of UniProt A0A2D2D0T8
- Elsewhere: RCSB PDB 7M8R · PDBe 7M8R · UniProt A0A2D2D5X0 · UniProt A0A2D2D5X7 · UniProt A0A2D2D0T0 · UniProt A0A2D2D0T8
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