Research workbench
P450 (oxya) from kistamicin biosynthesis, Y99F mutant
Analyse P450 (oxya) from kistamicin biosynthesis, Y99F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TTB
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cytochrome P450 hydroxylase
- UniProt
- A0A2P9IBF7
- Ligands
- HEM
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cytochrome P450 hydroxylase | protein | 354 | 55% helix, 11% strand | A0A2P9IBF7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 515 | 0.79 | 0.86 | 59 | HEM |
| 2 | 93 | 0.37 | 0.76 | 22 | empty |
| 3 | 53 | 0.35 | 0.79 | 13 | empty |
Compared structures
- 7TTB · P450 (OxyA) from kistamicin biosynthesis, Y99F mutant · 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 A0A2P9IBF7
- Elsewhere: RCSB PDB 7TTB · PDBe 7TTB · UniProt A0A2P9IBF7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.