Research workbench
Structure of rifampicin monooxygenase complexed with rifampicin
Analyse Structure of rifampicin monooxygenase complexed with rifampicin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KOX
- Type
- protein
- Length
- 473 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pentachlorophenol 4-monooxygenase
- EC
- 1.14.13.50
- UniProt
- A0A0H5NE66
- Ligands
- FAD, RFP
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pentachlorophenol 4-monooxygenase (EC 1.14.13.50) | protein | 473 | 33% helix, 23% strand | A0A0H5NE66 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1015 | 0.80 | 0.81 | 92 | FAD, RFP |
| 2 | 115 | 0.53 | 0.82 | 24 | empty |
| 3 | 87 | 0.38 | 0.77 | 17 | empty |
| 4 | 55 | 0.30 | 0.75 | 17 | empty |
| 5 | 63 | 0.29 | 0.74 | 14 | empty |
Compared structures
- 5KOX · Structure of rifampicin monooxygenase complexed with rifampicin · 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 A0A0H5NE66
- Elsewhere: RCSB PDB 5KOX · PDBe 5KOX · UniProt A0A0H5NE66
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