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Crystal structure of human cytochrome P450 3A4
Analyse Crystal structure of human cytochrome P450 3A4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W0E
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 3A4
- EC
- 1.14.13.67, 1.14.14.1
- UniProt
- P08684
- Ligands
- HEM
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 3A4 (EC 1.14.13.67, 1.14.14.1) | protein | 450 | 47% helix, 8% strand | P08684 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
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 | 995 | 0.86 | 0.87 | 93 | HEM |
| 2 | 227 | 0.51 | 0.75 | 29 | empty |
| 3 | 142 | 0.45 | 0.77 | 22 | empty |
| 4 | 57 | 0.35 | 0.78 | 14 | empty |
| 5 | 63 | 0.32 | 0.75 | 14 | 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 P08684
- Elsewhere: RCSB PDB 1W0E · PDBe 1W0E · UniProt P08684
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