Research workbench
Crystal structure of human CYP3A4 bound to ritonavir
Analyse Crystal structure of human CYP3A4 bound to ritonavir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VC0
- Type
- protein
- Length
- 463 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 3A4
- EC
- 1.14.13.157, 1.14.13.32, 1.14.13.67, 1.14.13.9
- UniProt
- P08684
- Ligands
- HEM, RIT
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 3A4 (EC 1.14.13.157, 1.14.13.32, 1.14.13.67, 1.14.13.9) | protein | 463 | 51% helix, 9% strand | P08684 |
Ligands and binding sites
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 | 1173 | 0.84 | 0.85 | 74 | HEM, RIT |
| 2 | 289 | 0.59 | 0.78 | 41 | empty |
| 3 | 108 | 0.45 | 0.78 | 28 | empty |
| 4 | 161 | 0.40 | 0.72 | 21 | empty |
| 5 | 75 | 0.36 | 0.77 | 20 | 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 5VC0 · PDBe 5VC0 · UniProt P08684
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