Research workbench
EGFR(T790M/V948R) in complex with LN2084
Analyse EGFR(T790M/V948R) in complex with LN2084 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V5N
- Type
- protein
- Length
- 1,213 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor
- EC
- 2.7.10.1
- UniProt
- P00533
- Ligands
- QP7, CL
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 308 | 42% helix, 16% strand | P00533 |
| A | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 314 | 41% helix, 16% strand | P00533 |
| B | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 297 | 41% helix, 17% strand | P00533 |
| C | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 294 | 43% helix, 17% strand | P00533 |
Ligands and binding sites
- QP7 · 3-[4-(4-fluorophenyl)-5-(2-phenyl-1H-pyrrolo[2,3-b]pyridin-4-yl)-1H-imidazol-2-yl]propan-1-ol · ligand · 4 copies · chains D, A, B, C
- CL · Chloride ion · ion · 4 copies · chains D, A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1155 | 0.84 | 0.85 | 99 | QP7, CL |
| 2 | 1143 | 0.83 | 0.84 | 102 | QP7, CL |
| 3 | 846 | 0.80 | 0.82 | 78 | QP7, CL |
| 4 | 499 | 0.71 | 0.80 | 63 | QP7, CL |
| 5 | 257 | 0.66 | 0.83 | 30 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1675 Ų buried · 18 hydrogen bonds · protein-protein
- D–C · 1671 Ų buried · 21 hydrogen bonds · protein-protein
- D–A · 630 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 353 Ų buried · 4 hydrogen bonds · protein-protein
- D–B · 71 Ų buried · 1 hydrogen bond · 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 P00533
- Elsewhere: RCSB PDB 6V5N · PDBe 6V5N · UniProt P00533
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.