MolNFT v1 · #146910 · protein
Structure of human cytochrome P450 1A1 with erlotinib
6DWN: “Structure of human cytochrome P450 1A1 with erlotinib”. X-ray diffraction, 3 ligands (HEM, AQ4, CPS), 20 pockets (best druggability 0.86). MolNFT v1 #146910 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DWN
- Type
- protein
- Length
- 1,856 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 1A1
- EC
- 1.14.14.1
- UniProt
- P04798
- Ligands
- HEM, AQ4, CPS
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 1A1 (EC 1.14.14.1) | protein | 476 | 53% helix, 10% strand | P04798 |
| B | Cytochrome P450 1A1 (EC 1.14.14.1) | protein | 465 | 54% helix, 10% strand | P04798 |
| C | Cytochrome P450 1A1 (EC 1.14.14.1) | protein | 462 | 53% helix, 10% strand | P04798 |
| D | Cytochrome P450 1A1 (EC 1.14.14.1) | protein | 453 | 53% helix, 10% strand | P04798 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- AQ4 · [6,7-bis(2-methoxy-ethoxy)quinazoline-4-yl]-(3-ethynylphenyl)amine · ligand · 4 copies · chains A, B, C, D
- CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · 2 copies · chains A, B
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 | 671 | 0.86 | 0.90 | 82 | HEM, AQ4 |
| 2 | 693 | 0.85 | 0.89 | 77 | HEM, AQ4 |
| 3 | 669 | 0.85 | 0.89 | 78 | HEM, AQ4 |
| 4 | 735 | 0.84 | 0.87 | 77 | HEM, AQ4 |
| 5 | 648 | 0.68 | 0.76 | 68 | empty |
Interfaces
4 interfaces between chains.
- A–B · 608 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 530 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 286 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 15 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 P04798
- Elsewhere: RCSB PDB 6DWN · PDBe 6DWN · UniProt P04798
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