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Human CK2 catalytic domain in complex with a benzopyridoindole derivative inhibitor

Analyse Human CK2 catalytic domain in complex with a benzopyridoindole derivative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OWL
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CSNK2A1 protein
UniProt: Q5U5J2
Ligands: 19E, SO4
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CSNK2A1 protein	protein	330	40% helix, 15% strand	Q5U5J2

Ligands and binding sites

19E · 11-chloro-8-methyl-7H-benzo[e]pyrido[4,3-b]indol-3-ol · ligand · chains A
SO4 · Sulfate ion · ion · 3 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	402	0.71	0.82	44	19E
2	50	0.59	0.92	19	empty
3	53	0.41	0.82	13	empty

Compared structures

3OWL · Human CK2 catalytic domain in complex with a benzopyridoindole derivative inhibitor · the same entry in another collection · chain A against A, TM-score 1.00

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 Q5U5J2
Elsewhere: RCSB PDB 3OWL · PDBe 3OWL · UniProt Q5U5J2

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