Research workbench
CDK2 in complex with inhibitor rc-2-13
Analyse CDK2 in complex with inhibitor rc-2-13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QTW
- Type
- protein
- Length
- 294 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-dependent kinase 2
- EC
- 2.7.11.22
- UniProt
- P24941
- Ligands
- X3A
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-dependent kinase 2 (EC 2.7.11.22) | protein | 294 | 32% helix, 13% strand | P24941 |
Ligands and binding sites
- X3A · [4-amino-2-(phenylamino)-1,3-thiazol-5-yl](pyridin-3-yl)methanone · ligand · chains A
- EDO · 1,2-ethanediol · additive · 6 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.76 | 0.91 | 28 | X3A |
| 2 | 142 | 0.67 | 0.88 | 29 | empty |
| 3 | 61 | 0.33 | 0.77 | 16 | empty |
| 4 | 52 | 0.33 | 0.77 | 11 | 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 3QTW · PDBe 3QTW · UniProt P24941
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