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Mechanism of phosphate transfer by nucleoside diphosphate kinase: X- ray structures of a phospho-histidine intermediate of the enzymes from drosophila and dictyostelium

Analyse Mechanism of phosphate transfer by nucleoside diphosphate kinase: X- ray… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NSP
Type: protein
Length: 150 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoside diphosphate kinase
EC: 2.7.4.6
UniProt: P22887
Pockets: 1 · best druggability 0.39

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleoside diphosphate kinase (EC 2.7.4.6)	protein	150	43% helix, 17% strand	P22887

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	106	0.39	0.76	22	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

1NSP · Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of a… · the same entry in another collection · chain A against A, TM-score 1.00
P22887 · AlphaFold monomer V2.0 prediction for nucleoside diphosphate kinase, cytosolic (P22887) · 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 P22887
Elsewhere: RCSB PDB 1NSP · PDBe 1NSP · UniProt P22887

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