GL1X · GenesisL1 explorer

Research workbench

The structure of the yeast sr protein kinase, SKY1P, with bound ADP

Analyse The structure of the yeast sr protein kinase, SKY1P, with bound ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Q8Y
Type
protein
Length
708 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sr protein kinase
EC
2.7.1.-
UniProt
Q03656
Ligands
ADP, ADE, MG, SO4
Pockets
10 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASr protein kinase (EC 2.7.1.-)protein35138% helix, 19% strandQ03656
BSr protein kinase (EC 2.7.1.-)protein35741% helix, 18% strandQ03656

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • ADE · Adenine · ligand · chains B
  • MG · Magnesium ion · metal · chains A
  • SO4 · Sulfate ion · ion · 8 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12550.640.8229MG, ADP
22090.550.7822ADE
31580.500.7816empty
4650.500.8521empty
5740.420.7914empty

Interfaces

1 interface between chains.

  • A–B · 607 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 1Q8Y · The structure of the yeast SR protein kinase, Sky1p, with bound ADP · the same entry in another collection · chain A against A, TM-score 1.00
  • Q03656 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase SKY1 (Q03656) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.