Research workbench
Human cyclin dependent kinase 2 complexed with the inhibitor 4-[4-(4-methyl-2-methylamino-thiazol-5-yl)- pyrimidin-2-ylamino]-phenol
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
- 1PXN
- Type
- protein
- Length
- 294 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
- CK6
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein kinase 2 (EC 2.7.1.-) | protein | 294 | 32% helix, 16% strand | P24941 |
Ligands and binding sites
- CK6 · 4-[4-(4-methyl-2-methylamino-thiazol-5-yl)-pyrimidin-2-ylamino]-phenol · 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 | 427 | 0.73 | 0.83 | 54 | CK6 |
| 2 | 55 | 0.26 | 0.73 | 12 | 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 1PXN · PDBe 1PXN · UniProt P24941
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