Research workbench
Insulin receptor kinase complexed with an inhibitor
Analyse Insulin receptor kinase complexed with an inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EKK
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin receptor
- EC
- 2.7.10.1
- UniProt
- P06213
- Ligands
- GS2
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin receptor (EC 2.7.10.1) | protein | 285 | 38% helix, 17% strand | P06213 |
Ligands and binding sites
- GS2 · 2-[(2-{[1-(N,N-dimethylglycyl)-5-methoxy-1H-indol-6-yl]amino}-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-6-fluoro-N-methylbenzamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.62 | 0.80 | 37 | GS2 |
| 2 | 105 | 0.44 | 0.78 | 23 | empty |
| 3 | 93 | 0.35 | 0.75 | 17 | 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 P06213
- Elsewhere: RCSB PDB 3EKK · PDBe 3EKK · UniProt P06213
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