Research workbench

AlphaFold monomer V2.0 prediction for nucleoside diphosphate kinase B (P22392)

Analyse AlphaFold monomer V2.0 prediction for nucleoside diphosphate kinase B (P22392) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P22392
Type: protein
Length: 152 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
Molecule: Nucleoside diphosphate kinase B
UniProt: P22392
Pockets: 1 · best druggability 0.48

Structure

1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleoside diphosphate kinase B	protein	152	49% helix, 16% strand	P22392

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	177	0.48	0.77	25	empty

Compared structures

7KPF · NME2 bound to myristoyl-CoA · an experimental structure of the same protein · chain A against A, TM-score 1.00
7KPF · NME2 bound to myristoyl-CoA · an experimental structure of the same protein · chain A against A, TM-score 1.00
8PYW · Crystal structure of the human Nucleoside-diphosphate kinase B domain bound to compound… · an experimental structure of the same protein · chain A against F, TM-score 1.00
8PIE · Crystal structure of the human nucleoside diphosphate kinase B domain in complex with the… · an experimental structure of the same protein · chain A against E, 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 P22392
Elsewhere: UniProt P22392 · AlphaFold DB P22392

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