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Crystal structure of a binary complex of protein kinase CK2 (alpha-subunit) and mg-amppnp

Analyse Crystal structure of a binary complex of protein kinase CK2 (alpha-subunit) and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DAW
Type
protein
Length
327 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein kinase CK2
EC
2.7.1.37
UniProt
P28523
Ligands
ANP, MG
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein kinase CK2 (EC 2.7.1.37)protein32743% helix, 15% strandP28523

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
  • MG · Magnesium ion · metal · 2 copies · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13270.690.8244MG, ANP
2510.630.9418empty
3580.460.8418empty

Compared structures

  • 1DAW · Crystal structure of a binary complex of protein kinase CK2 (alpha-subunit) and mg-amppnp · the same entry in another collection · chain A against A, TM-score 1.00
  • P28523 · AlphaFold monomer V2.0 prediction for casein kinase II subunit alpha (P28523) · a predicted model of the same protein · chain A against A, TM-score 0.99

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