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Structure of apo human NEK7

Analyse Structure of apo human NEK7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WQM
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase NEK7
EC: 2.7.11.1
UniProt: Q8TDX7
Ligands: NI, SO4
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase NEK7 (EC 2.7.11.1)	protein	258	43% helix, 17% strand	Q8TDX7

Ligands and binding sites

NI · Nickel (II) ion · metal · chains A
SO4 · Sulfate ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	140	0.47	0.77	26	empty
2	89	0.41	0.78	17	empty
3	105	0.40	0.75	17	empty

Compared structures

2WQM · Structure of apo human Nek7 · the same entry in another collection · chain A against A, TM-score 1.00
Q8TDX7 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase NEK7 (Q8TDX7) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q8TDX7
Elsewhere: RCSB PDB 2WQM · PDBe 2WQM · UniProt Q8TDX7

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