Research workbench
Human cyclin-dependent kinase 2 phosphorylated on thr 160
Analyse Human cyclin-dependent kinase 2 phosphorylated on thr 160 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B39
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (cell division protein kinase 2)
- EC
- 2.7.1.37
- UniProt
- P24941
- Ligands
- ACE, ATP, MG
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (cell division protein kinase 2) (EC 2.7.1.37) | protein | 290 | 36% helix, 16% strand | P24941 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.71 | 0.84 | 38 | MG, ATP |
| 2 | 67 | 0.35 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 1B39 · PDBe 1B39 · UniProt P24941
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