Research workbench
CKSHS1: human cyclin dependent kinase subunit, type 1 in complex with phosphate
Analyse CKSHS1: human cyclin dependent kinase subunit, type 1 in complex with phosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DKS
- Type
- protein
- Length
- 149 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin dependent kinase subunit, type 1
- UniProt
- P61024
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin dependent kinase subunit, type 1 | protein | 76 | 13% helix, 29% strand | P61024 |
| B | Cyclin dependent kinase subunit, type 1 | protein | 73 | 16% helix, 29% strand | P61024 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.38 | 0.76 | 18 | PO4 |
| 2 | 57 | 0.32 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 525 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1DKS · CKSHS1: human cyclin dependent kinase subunit, type 1 in complex with phosphate · the same entry in another collection · chain A against A, TM-score 1.00
- P61024 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinases regulatory subunit 1… · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P61024
- Elsewhere: RCSB PDB 1DKS · PDBe 1DKS · UniProt P61024
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