Research workbench
CDK2 in complex with FRAGLITE14
Analyse CDK2 in complex with FRAGLITE14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q4A
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-dependent kinase 2
- UniProt
- P24941
- Ligands
- HGW
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-dependent kinase 2 | protein | 292 | 35% helix, 16% strand | P24941 |
Ligands and binding sites
- HGW · 5-iodanylpyrimidine · 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 | 317 | 0.67 | 0.81 | 35 | HGW |
| 2 | 81 | 0.42 | 0.79 | 18 | empty |
| 3 | 87 | 0.39 | 0.77 | 17 | empty |
| 4 | 65 | 0.33 | 0.76 | 20 | 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 6Q4A · PDBe 6Q4A · UniProt P24941
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