MolNFT v1 · #48015 · protein
Crystal structure of human microsomal P450 2A6 L240C/N297Q
2PG6 · Cytochrome P450 2A6: “Crystal structure of human microsomal P450 2A6 L240C/N297Q”. X-ray diffraction, 1 ligand (HEM), 16 pockets (best druggability 0.86). MolNFT v1 #48015 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2PG6
- 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
- Pockets
- 16 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 54% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 2A6 (EC 1.14.14.1) | protein | 465 | 52% helix, 10% strand | P11509 |
| B | Cytochrome P450 2A6 (EC 1.14.14.1) | protein | 464 | 54% helix, 10% strand | P11509 |
| C, D | Cytochrome P450 2A6 (EC 1.14.14.1) | protein | 464 | 54% helix, 10% strand | P11509 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.86 | 0.93 | 47 | HEM |
| 2 | 418 | 0.86 | 0.93 | 45 | HEM |
| 3 | 404 | 0.85 | 0.93 | 43 | HEM |
| 4 | 450 | 0.85 | 0.92 | 54 | HEM |
| 5 | 895 | 0.78 | 0.80 | 85 | empty |
Interfaces
5 interfaces between chains.
- A–B · 666 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 421 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 407 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 196 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 171 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 2PG6 · PDBe 2PG6 · UniProt P11509
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