Research workbench
Structure of CDK2 with a 3-hydroxychromones
Analyse Structure of CDK2 with a 3-hydroxychromones in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DUV
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein kinase 2
- EC
- 2.7.11.22
- UniProt
- P24941
- Ligands
- 371
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein kinase 2 (EC 2.7.11.22) | protein | 272 | 33% helix, 17% strand | P24941 |
Ligands and binding sites
- 371 · 2-(3,4-dihydroxyphenyl)-8-(1,1-dioxidoisothiazolidin-2-yl)-3-hydroxy-6-methyl-4H-chromen-4-one · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.67 | 0.83 | 25 | 371 |
| 2 | 59 | 0.44 | 0.82 | 23 | empty |
| 3 | 50 | 0.37 | 0.80 | 18 | empty |
| 4 | 53 | 0.31 | 0.76 | 17 | 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 2DUV · PDBe 2DUV · UniProt P24941
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