Research workbench
Human cytochrome P450 2A6 in complex with nicotine
Analyse Human cytochrome P450 2A6 in complex with nicotine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EJJ
- Type
- protein
- Length
- 1,857 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, NCT
- Pockets
- 18 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 2A6 (EC 1.14.14.1) | protein | 465 | 53% helix, 11% strand | P11509 |
| B, C, D | Cytochrome P450 2A6 (EC 1.14.14.1) | protein | 464 | 52% helix, 10% strand | P11509 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- NCT · (S)-3-(1-methylpyrrolidin-2-yl)pyridine · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 435 | 0.86 | 0.93 | 47 | HEM, NCT |
| 2 | 409 | 0.86 | 0.94 | 44 | HEM, NCT |
| 3 | 415 | 0.86 | 0.93 | 43 | HEM, NCT |
| 4 | 459 | 0.84 | 0.91 | 52 | NCT, HEM |
| 5 | 382 | 0.57 | 0.75 | 35 | empty |
Interfaces
3 interfaces between chains.
- A–B · 433 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 262 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 212 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 4EJJ · PDBe 4EJJ · UniProt P11509
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.