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NEK2 kinase bound to inhibitor 102

Analyse NEK2 kinase bound to inhibitor 102 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SGK
Type: protein
Length: 247 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase NEK2
EC: 2.7.11.1
UniProt: P51955
Ligands: LCQ
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase NEK2 (EC 2.7.11.1)	protein	247	45% helix, 19% strand	P51955

Ligands and binding sites

LCQ · 2-phenylazanyl-9~{H}-purine-6-carbonitrile · 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	361	0.62	0.77	41	LCQ
2	52	0.32	0.77	11	empty
3	66	0.30	0.74	21	empty

Compared structures

6SGK · Nek2 kinase bound to inhibitor 102 · the same entry in another collection · chain A against A, TM-score 1.00
P51955 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase NEK2 (P51955) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P51955
Elsewhere: RCSB PDB 6SGK · PDBe 6SGK · UniProt P51955

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