MolNFT v1 · #17022 · protein
Structure of human cytochrome P450 CYP2C9
1OG2 · Cytochrome P450 2C9: “Structure of human cytochrome P450 CYP2C9”. X-ray diffraction, 1 ligand (HEC), 8 pockets (best druggability 0.87). MolNFT v1 #17022 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OG2
- Type
- protein
- Length
- 922 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 2C9
- EC
- 1.14.13.80, 1.14.13.48, 1.14.13.49
- UniProt
- P11712
- Ligands
- HEC
- Pockets
- 8 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome P450 2C9 (EC 1.14.13.80, 1.14.13.48, 1.14.13.49) | protein | 461 | 53% helix, 9% strand | P11712 |
Ligands and binding sites
- HEC · Heme C · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 957 | 0.87 | 0.89 | 82 | HEC |
| 2 | 1050 | 0.87 | 0.88 | 92 | HEC |
| 3 | 1043 | 0.78 | 0.80 | 85 | empty |
| 4 | 134 | 0.49 | 0.79 | 24 | empty |
| 5 | 138 | 0.47 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 650 Ų buried · 6 hydrogen bonds · protein-protein
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 P11712
- Elsewhere: RCSB PDB 1OG2 · PDBe 1OG2 · UniProt P11712
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