Research workbench
Crystal structure of CYP105P1 wild-type 4-phenylimidazole complex
Analyse Crystal structure of CYP105P1 wild-type 4-phenylimidazole complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E5K
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 (cytochrome P450 hydroxylase)
- UniProt
- Q93H81
- Ligands
- HEM, PIM
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 (cytochrome P450 hydroxylase) | protein | 382 | 51% helix, 11% strand | Q93H81 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- PIM · 4-phenyl-1H-imidazole · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 957 | 0.82 | 0.83 | 93 | HEM, PIM |
| 2 | 192 | 0.66 | 0.85 | 29 | empty |
Compared structures
- 3E5K · Crystal structure of CYP105P1 wild-type 4-phenylimidazole complex · 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 Q93H81
- Elsewhere: RCSB PDB 3E5K · PDBe 3E5K · UniProt Q93H81
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.