MolNFT v1 · #159435 · protein
HER3 pseudokinase domain bound to bosutinib
6OP9 · Receptor tyrosine-protein kinase erbb-3: “HER3 pseudokinase domain bound to bosutinib”. X-ray diffraction, 1 ligand (DB8), 2 pockets (best druggability 0.70). MolNFT v1 #159435 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6OP9
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor tyrosine-protein kinase erbb-3
- EC
- 2.7.10.1
- UniProt
- P21860
- Ligands
- DB8
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor tyrosine-protein kinase erbb-3 (EC 2.7.10.1) | protein | 276 | 39% helix, 18% strand | P21860 |
Ligands and binding sites
- DB8 · 4-[(2,4-dichloro-5-methoxyphenyl)amino]-6-methoxy-7-[3-(4-methylpiperazin-1-yl)propoxy]quinoline-3-carbonitrile · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 486 | 0.70 | 0.80 | 52 | DB8 |
| 2 | 168 | 0.46 | 0.75 | 26 | empty |
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 P21860
- Elsewhere: RCSB PDB 6OP9 · PDBe 6OP9 · UniProt P21860
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