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Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 16a

Analyse Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 16a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6S9W
Type
protein
Length
411 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.3
Source
Homo sapiens
Molecule
RAC-alpha serine/threonine-protein kinase
EC
2.7.11.1
UniProt
P31749
Ligands
L1Z
Pockets
3 · best druggability 0.81

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 33% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARAC-alpha serine/threonine-protein kinase (EC 2.7.11.1)protein41133% helix, 24% strandP31749

Ligands and binding sites

  • L1Z · ~{N}-[3-[1-[[4-(5-methyl-6-oxidanylidene-3-phenyl-1~{H}-pyrazin-2-yl)phenyl]methyl]piperidin-4-yl]-2-oxidanylidene-1~{H}-benzimidazol-5-yl]propanamide · 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111500.810.82101L1Z
24380.670.7947empty
31120.510.8120empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 6S9W · Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 16A · 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 0.68

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