Research workbench
Human cytochrome P450 2A6 in complex with pilocarpine
Analyse Human cytochrome P450 2A6 in complex with pilocarpine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T3R
- Type
- protein
- Length
- 1,853 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 2A6
- EC
- 1.14.14.1
- UniProt
- P11509
- Ligands
- HEM, 9PL
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Cytochrome P450 2A6 (EC 1.14.14.1) | protein | 463 | 53% helix, 10% strand | P11509 |
| D | Cytochrome P450 2A6 (EC 1.14.14.1) | protein | 464 | 52% helix, 9% strand | P11509 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- 9PL · (3S,4R)-3-ethyl-4-[(1-methyl-1H-imidazol-5-yl)methyl]dihydrofuran-2(3H)-one · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 427 | 0.86 | 0.94 | 46 | HEM, 9PL |
| 2 | 440 | 0.86 | 0.93 | 46 | HEM, 9PL |
| 3 | 433 | 0.86 | 0.93 | 48 | HEM, 9PL |
| 4 | 461 | 0.85 | 0.92 | 52 | HEM, 9PL |
| 5 | 838 | 0.73 | 0.78 | 69 | empty |
Interfaces
5 interfaces between chains.
- A–D · 429 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 420 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 356 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 127 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 67 Ų buried · 0 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 P11509
- Elsewhere: RCSB PDB 3T3R · PDBe 3T3R · UniProt P11509
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