Research workbench
Human CYP3A4 bound to an inhibitor
Analyse Human CYP3A4 bound to an inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UFC
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 3A4
- EC
- 1.14.14.1, 1.14.14.56, 1.14.14.73, 1.14.14.55
- UniProt
- P08684
- Ligands
- HEM, NJO
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 3A4 (EC 1.14.14.1, 1.14.14.56, 1.14.14.73, 1.14.14.55) | protein | 461 | 51% helix, 10% strand | P08684 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- NJO · (2R)-3-phenyl-2-({(2S)-3-phenyl-2-[3-(pyridin-3-yl) propanamido]propyl}sulfanyl)-N-[2-(pyridin-3-yl) ethyl]propanamide · 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 | 1087 | 0.86 | 0.86 | 80 | HEM, NJO |
| 2 | 181 | 0.54 | 0.79 | 28 | empty |
| 3 | 234 | 0.48 | 0.73 | 30 | empty |
| 4 | 171 | 0.46 | 0.75 | 31 | empty |
| 5 | 53 | 0.27 | 0.73 | 16 | 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 7UFC · PDBe 7UFC · UniProt P08684
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