MolNFT v1 · #32548 · protein
Structure of CDK2 complexed with pnu-230032
2BTS · Cell division protein kinase 2: “Structure of CDK2 complexed with pnu-230032”. X-ray diffraction, 1 ligand (U32), 3 pockets (best druggability 0.69). MolNFT v1 #32548 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2BTS
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein kinase 2
- EC
- 2.7.1.37
- UniProt
- P24941
- Ligands
- U32
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein kinase 2 (EC 2.7.1.37) | protein | 274 | 36% helix, 17% strand | P24941 |
Ligands and binding sites
- U32 · 4-[(5-isopropyl-1,3-thiazol-2-yl)amino]benzenesulfonamide · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.69 | 0.83 | 33 | U32 |
| 2 | 190 | 0.62 | 0.83 | 27 | empty |
| 3 | 61 | 0.27 | 0.73 | 14 | 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 2BTS · PDBe 2BTS · UniProt P24941
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