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Crystal structure of the apo form of the unphosphorylated human death associated protein kinase 3 (DAPK3)

Analyse Crystal structure of the apo form of the unphosphorylated human death… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A6O
Type
protein
Length
531 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.6
Source
HOMO SAPIENS
Molecule
Death-associated protein kinase 3
EC
2.7.11.1
UniProt
O43293
Pockets
7 · best druggability 0.77

Structure

x-ray diffraction · resolution 1.6 · 2 distinct chains · 37% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADeath-associated protein kinase 3 (EC 2.7.11.1)protein26538% helix, 20% strandO43293
BDeath-associated protein kinase 3 (EC 2.7.11.1)protein26637% helix, 20% strandO43293

Ligands and binding sites

  • GOL · Glycerol · additive · 3 copies · chains A, B
  • PGO · S-1,2-propanediol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15740.770.8369GOL
21590.620.8320GOL
31410.610.8423GOL
4630.440.8317empty
51440.400.7325empty

Interfaces

1 interface between chains.

  • A–B · 2287 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 5A6O · Crystal structure of the apo form of the unphosphorylated human death associated protein… · the same entry in another collection · chain A against A, TM-score 1.00
  • O43293 · AlphaFold monomer V2.0 prediction for death-associated protein kinase 3 (O43293) · a predicted model of the same protein · chain A against A, TM-score 0.93

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