Research workbench
Human IGF in complex with a Dyrk1B inhibitor
Analyse Human IGF in complex with a Dyrk1B inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D2R
- Type
- protein
- Length
- 300 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- HOMO SAPIENS
- Molecule
- Insulin-like growth factor 1 receptor
- EC
- 2.7.10.1
- UniProt
- P08069
- Ligands
- DYK, CL
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin-like growth factor 1 receptor (EC 2.7.10.1) | protein | 300 | 39% helix, 18% strand | P08069 |
Ligands and binding sites
- DYK · N-{2-methoxy-4-[(1-methylpiperidin-4-yl)oxy]phenyl}-4-(1H-pyrrolo[2,3-c]pyridin-3-yl)pyrimidin-2-amine · ligand · chains A
- CL · Chloride ion · ion · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.65 | 0.83 | 30 | DYK |
| 2 | 152 | 0.44 | 0.75 | 26 | empty |
| 3 | 69 | 0.36 | 0.77 | 18 | empty |
| 4 | 110 | 0.35 | 0.73 | 18 | 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 P08069
- Elsewhere: RCSB PDB 4D2R · PDBe 4D2R · UniProt P08069
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