Research workbench
P450ERYF/KETOCONAZOLE
Analyse P450ERYF/KETOCONAZOLE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JIN
- Type
- protein
- Length
- 403 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 107A1
- EC
- 1.-.-.-
- UniProt
- Q00441
- Ligands
- HEM, KTN
- Pockets
- 2 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 107A1 (EC 1.-.-.-) | protein | 403 | 51% helix, 10% strand | Q00441 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- KTN · Cis-1-acetyl-4-(4-((2-(2,4-dichlorophenyl)-2-(1H-imidazol-1-ylmethyl)-1,3-dioxolan-4-yl)methoxy)phenyl)piperazine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.87 | 0.89 | 66 | HEM, KTN |
| 2 | 111 | 0.40 | 0.76 | 18 | empty |
Compared structures
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 Q00441
- Elsewhere: RCSB PDB 1JIN · PDBe 1JIN · UniProt Q00441
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