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Crystal structure of maize CK2 alpha in complex with iqa

Analyse Crystal structure of maize CK2 alpha in complex with iqa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OM1
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Casein kinase II, alpha chain
EC: 2.7.1.37
UniProt: P28523
Ligands: IQA
Pockets: 2 · best druggability 0.70

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Casein kinase II, alpha chain (EC 2.7.1.37)	protein	325	43% helix, 15% strand	P28523

Ligands and binding sites

IQA · (5-oxo-5,6-dihydro-indolo[1,2-a]quinazolin-7-yl)-acetic acid · ligand · chains A

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

Pockets

2 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	338	0.70	0.83	47	IQA
2	51	0.30	0.76	15	empty

Compared structures

1OM1 · Crystal structure of maize CK2 alpha in complex with IQA · 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

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 P28523
Elsewhere: RCSB PDB 1OM1 · PDBe 1OM1 · UniProt P28523

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