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Spirochromane AKT inhibitors

Analyse Spirochromane AKT inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QKL
Type
protein
Length
328 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rac-alpha SERINE/THREONINE-protein kinase; Gsk-3 beta peptide
EC
2.7.11.1
UniProt
P31749
Ligands
SMR
Pockets
3 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARac-alpha SERINE/THREONINE-protein kinase (EC 2.7.11.1)protein31835% helix, 17% strandP31749
CGsk-3 beta peptideprotein100% helix, 20% strand—

Ligands and binding sites

  • SMR · N-{(2S)-3-[(3S)-8',9'-dihydro-1H,3'H-spiro[piperidine-3,7'-pyrano[3,2-e]indazol]-1-yl]-2-hydroxypropyl}-N-(2-ethoxyethyl)-2,6-dimethylbenzenesulfonamide · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16850.810.8562SMR
2660.410.8019empty
3510.300.7718empty

Interfaces

1 interface between chains.

  • A–C · 665 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 3QKL · Spirochromane Akt Inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
  • P31749 · AlphaFold monomer V2.0 prediction for rac-alpha SERINE/THREONINE- protein kinase (P31749) · a predicted model of the same protein · chain A against A, TM-score 0.98

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