Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control.

Rosano C, Sabini E, Rizzi M, Deriu D, Murshudov G, Bianchi M, Serafini G, Magnani M, Bolognesi M

Hexokinase I sets the pace of glycolysis in the brain, catalyzing the ATP-dependent phosphorylation of glucose. The catalytic properties of hexokinase I are dependent on product inhibition as well as on the action of phosphate. In vivo, a large fraction of hexokinase I is bound to the mitochondrial outer membrane, where the enzyme adopts a tetrameric assembly. The mitochondrion-bound hexokinase ... [more]

Structure Nov. 15, 1999; 7(11);1427-37 [Pubmed: 10574795]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
HK1 HK1	Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.	Liu X (2018)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

HK1

Gene Ontology Biological Process

Gene Ontology Molecular Function

fructokinase activity [IBA]glucokinase activity [IBA]hexokinase activity [TAS]mannokinase activity [IBA]protein binding [IPI]

Gene Ontology Cellular Component

HK1