UniProt A0A2P9IBF7
cytochrome P450 hydroxylase (A0A2P9IBF7)
cytochrome P450 hydroxylase (UniProt A0A2P9IBF7), EC 1.-.-.-: 12 experimental structures on GenesisL1, 1 ligand bound, 9 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A2P9IBF7
- Protein
- cytochrome P450 hydroxylase
- EC
- 1.-.-.-
- Experimental structures
- 12
- Predicted models
- 0
- Ligands
- 1
- Pockets
- 9 · 4 records with a druggable one
Structures
12 records of A0A2P9IBF7 in the MolNFT archive: 12 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 6M7L | Complex of OxyA with the X-domain from GPA biosynthesis | x-ray diffraction | A | HEM | — |
| 6M7L | Complex of oxya with the X-domain from gpa biosynthesis | x-ray diffraction | A | HEM | — |
| 7TTA | P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation, attenuated beam | x-ray diffraction | A | HEM | 1 (best 0.79) |
| 7TTA | P450 (oxya) from kistamicin biosynthesis, mixed heme conformation, attenuated beam | x-ray diffraction | A | HEM | — |
| 7TTB | P450 (OxyA) from kistamicin biosynthesis, Y99F mutant | x-ray diffraction | A | HEM | — |
| 7TTB | P450 (oxya) from kistamicin biosynthesis, Y99F mutant | x-ray diffraction | A | HEM | — |
| 7TTO | P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation | x-ray diffraction | A | HEM | 2 (best 0.80) |
| 7TTO | P450 (oxya) from kistamicin biosynthesis, mixed heme conformation | x-ray diffraction | A | HEM | — |
| 7TTP | P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation | x-ray diffraction | A | HEM | 3 (best 0.79) |
| 7TTP | P450 (oxya) from kistamicin biosynthesis, mixed heme conformation | x-ray diffraction | A | HEM | — |
| 7TTQ | P450 (OxyA) from kistamicin biosynthesis, imidazole complex | x-ray diffraction | A | HEM | 3 (best 0.80) |
| 7TTQ | P450 (oxya) from kistamicin biosynthesis, imidazole complex | x-ray diffraction | A | HEM | — |
Ligands
- HEM · Protoporphyrin IX containing Fe · in 12 records
Elsewhere
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