Research workbench
HIPK2 kinase domain bound to cx-4945
Analyse HIPK2 kinase domain bound to cx-4945 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P5S
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homeodomain-interacting protein kinase 2
- EC
- 2.7.11.1
- UniProt
- Q9H2X6
- Ligands
- 3NG
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homeodomain-interacting protein kinase 2 (EC 2.7.11.1) | protein | 333 | 42% helix, 18% strand | Q9H2X6 |
Ligands and binding sites
- 3NG · 5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid · 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 | 241 | 0.56 | 0.78 | 21 | 3NG |
| 2 | 124 | 0.49 | 0.79 | 23 | empty |
| 3 | 54 | 0.31 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 2 modified (phosphorylation).
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 Q9H2X6
- Elsewhere: RCSB PDB 6P5S · PDBe 6P5S · UniProt Q9H2X6
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