MolNFT v1 · #12350 · protein
Cyclin-dependent kinase 2 (CDK2) complexed with 4-{[(2-oxo-1,2- dihydro-3H-indol-3-YLIDENE)METHYL]AMINO}-N-(1,3-thiazol-2-yl) benzenesulfonamide
1KE8 · Cell division protein kinase 2: “Cyclin-dependent kinase 2 (CDK2) complexed with 4-{[(2-oxo-1,2…”. X-ray diffraction, 1 ligand (LS4), 1 pocket (best druggability 0.67). MolNFT v1 #12350 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1KE8
- Type
- protein
- Length
- 282 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
- LS4
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein kinase 2 (EC 2.7.1.37) | protein | 282 | 35% helix, 17% strand | P24941 |
Ligands and binding sites
- LS4 · 4-{[(2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]amino}-N-(1,3-thiazol-2-yl)benzenesulfonamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 282 | 0.67 | 0.83 | 38 | LS4 |
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 1KE8 · PDBe 1KE8 · UniProt P24941
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