Research workbench
Crystal structure of HPK1 in complex with compound 2
Analyse Crystal structure of HPK1 in complex with compound 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R9L
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hematopoietic progenitor kinase
- EC
- 2.7.11.1
- UniProt
- Q92918
- Ligands
- 2YE
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hematopoietic progenitor kinase (EC 2.7.11.1) | protein | 282 | 42% helix, 16% strand | Q92918 |
Ligands and binding sites
- 2YE · 2-amino-N,N-dimethyl-5-(1H-pyrrolo[2,3-b]pyridin-5-yl) benzamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.61 | 0.79 | 50 | 2YE |
| 2 | 263 | 0.50 | 0.74 | 36 | empty |
Compared structures
- 7R9L · Crystal structure of HPK1 in complex with compound 2 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q92918
- Elsewhere: RCSB PDB 7R9L · PDBe 7R9L · UniProt Q92918
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