Research workbench
Wild type EGFR in complex with LN2899
Analyse Wild type EGFR in complex with LN2899 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VHP
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00533
- Ligands
- QP1
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 308 | — | P00533 |
Ligands and binding sites
- QP1 · N-{3-[(4-{4-(4-fluorophenyl)-2-[(2-methoxyethyl) sulfanyl]-1H-imidazol-5-yl}pyridin-2-yl)amino]-4-methoxyphenyl}propanamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P00533
- Elsewhere: RCSB PDB 6VHP · PDBe 6VHP · UniProt P00533
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