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Crystal structure of the CK2ALPHA/COMPOUND10 complex

Analyse Crystal structure of the CK2ALPHA/COMPOUND10 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WIK
Type: protein
Length: 334 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Casein kinase II subunit alpha
EC: 2.7.11.1
UniProt: P68400
Ligands: LCT
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Casein kinase II subunit alpha (EC 2.7.11.1)	protein	334	41% helix, 15% strand	P68400

Ligands and binding sites

LCT · N-[5-(4-nitrophenyl)-1,3,4-thiadiazol-2-yl]acetamide · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	250	0.65	0.82	31	LCT
2	64	0.35	0.77	15	empty
3	50	0.29	0.75	13	empty

Compared structures

3WIK · Crystal structure of the CK2alpha/compound10 complex · the same entry in another collection · chain A against A, TM-score 1.00
P68400 · AlphaFold monomer V2.0 prediction for casein kinase II subunit alpha (P68400) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P68400
Elsewhere: RCSB PDB 3WIK · PDBe 3WIK · UniProt P68400

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