Research workbench
Crystal structure of EGFR kinase domain T790M mutation in complex with AEE788
Analyse Crystal structure of EGFR kinase domain T790M mutation in complex with AEE788 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JIU
- Type
- protein
- Length
- 612 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor
- EC
- 2.7.1.112
- UniProt
- P00533
- Ligands
- AEE
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor (EC 2.7.1.112) | protein | 303 | 34% helix, 17% strand | P00533 |
| B | Epidermal growth factor receptor (EC 2.7.1.112) | protein | 309 | 35% helix, 16% strand | P00533 |
Ligands and binding sites
- AEE · 6-{4-[(4-ethylpiperazin-1-yl)methyl]phenyl}-N-[(1R)-1-phenylethyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 810 | 0.72 | 0.77 | 88 | AEE |
| 2 | 469 | 0.70 | 0.81 | 57 | empty |
| 3 | 105 | 0.43 | 0.78 | 20 | empty |
| 4 | 132 | 0.38 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1099 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2JIU · Crystal structure of EGFR kinase domain T790M mutation in complex with AEE788 · the same entry in another collection · chain A against A, TM-score 1.00
- P00533 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor (P00533) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 2JIU · PDBe 2JIU · UniProt P00533
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