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Crystal structure of amppnp bound CK2 alpha from C. neoformans

Analyse Crystal structure of amppnp bound CK2 alpha from C. neoformans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ISE
Type
protein
Length
654 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Casein kinase II subunit alpha
UniProt
A0A226BA59
Ligands
ANP, SO4
Pockets
6 · best druggability 0.72

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
B, ACasein kinase II subunit alphaprotein32743% helix, 15% strandA0A226BA59

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains B, A
  • SO4 · Sulfate ion · ion · 4 copies · chains B, A
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14990.720.8152SO4, ANP
24460.710.8154SO4, ANP
3600.440.8214empty
4550.390.8113empty
51220.370.7317empty

Interfaces

1 interface between chains.

  • B–A · 284 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 6ISE · Crystal structure of AMPPNP bound CK2 alpha from C. neoformans · the same entry in another collection · chain B against B, TM-score 1.00

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