MolNFT v1 · #36177 · protein
Human CDK2 in complex with isopentenyladenine
2EXM · Cell division protein kinase 2: “Human CDK2 in complex with isopentenyladenine”. X-ray diffraction, 1 ligand (ZIP), 1 pocket (best druggability 0.64). MolNFT v1 #36177 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2EXM
- Type
- protein
- Length
- 298 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
- ZIP
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein kinase 2 (EC 2.7.1.37) | protein | 298 | 34% helix, 16% strand | P24941 |
Ligands and binding sites
- ZIP · N-(3-methylbut-2-en-1-yl)-9H-purin-6-amine · 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 | 0.64 | 0.81 | 40 | ZIP |
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 2EXM · PDBe 2EXM · UniProt P24941
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