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Human cyclin dependent kinase 2 complexed with the inhibitor N-[4-(2,4-dimethyl-thiazol-5-YL)PYRIMIDIN-2-yl]- N'-hydroxyiminoformamide
Analyse Human cyclin dependent kinase 2 complexed with the inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PXK
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein kinase 2
- EC
- 2.7.1.-
- UniProt
- P24941
- Ligands
- CK3
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein kinase 2 (EC 2.7.1.-) | protein | 290 | 33% helix, 16% strand | P24941 |
Ligands and binding sites
- CK3 · N-[4-(2,4-dimethyl-1,3-thiazol-5-yl)pyrimidin-2-yl]-N'-hydroxyimidoformamide · 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 | 403 | 0.70 | 0.81 | 48 | CK3 |
| 2 | 64 | 0.27 | 0.72 | 13 | 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 P24941
- Elsewhere: RCSB PDB 1PXK · PDBe 1PXK · UniProt P24941
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