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Crystal structure of the cell cycle regulatory protein CKS1

Analyse Crystal structure of the cell cycle regulatory protein CKS1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QB3
Type
protein
Length
341 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cyclin-dependent kinases regulatory subunit
UniProt
P20486
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACyclin-dependent kinases regulatory subunitprotein11334% helix, 20% strandP20486
BCyclin-dependent kinases regulatory subunitprotein11934% helix, 8% strandP20486
CCyclin-dependent kinases regulatory subunitprotein10928% helix, 21% strandP20486

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13750.620.7746empty
2900.420.7922empty
3650.280.7315empty

Interfaces

3 interfaces between chains.

  • A–C · 2342 Ų buried · 45 hydrogen bonds · protein-protein
  • B–C · 283 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 93 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1QB3 · Crystal structure of the cell cycle regulatory protein CKS1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P20486 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinases regulatory subunit (P20486) · a predicted model of the same protein · chain C against A, TM-score 0.77

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