Research workbench
Structure of human cytochrome P450 CYP2C9
Analyse Structure of human cytochrome P450 CYP2C9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OG5
- 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, SWF
- Pockets
- 8 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 52% 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 | 52% helix, 9% strand | P11712 |
Ligands and binding sites
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 | 980 | 0.88 | 0.89 | 81 | HEC, SWF |
| 2 | 1048 | 0.88 | 0.89 | 89 | HEC, SWF |
| 3 | 1120 | 0.78 | 0.80 | 94 | empty |
| 4 | 165 | 0.49 | 0.77 | 24 | empty |
| 5 | 150 | 0.46 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 646 Ų buried · 7 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 1OG5 · PDBe 1OG5 · UniProt P11712
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