Literature summary for 2.7.2.3 extracted from

Palmai, Z.; Seifert, C.; Graeter, F.; Balog, E.
An allosteric signaling pathway of human 3-phosphoglycerate kinase from force distribution analysis (2014), PLoS Comput. Biol., 10, e1003444.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Synonyms

Synonyms	Comment	Organism
3-phosphoglycerate kinase	-	Homo sapiens
PGK	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	indispensable for the phosphoryl transfer reaction is a large conformational change from an inactive open to an active closed conformation via a hinge motion that should bring substrates into close proximity, molecular dynamics simulations, network-like representation of significant changes in inter-atomic forces, hydrogen-bond network in hinge bending region of apo and complexed hPGK, overview	Homo sapiens
physiological function	3-phosphogycerate kinase is a two domain enzyme, which transfers a phosphate group between its two substrates, 1,3-bisphosphoglycerate bound to the N-domain and ADP bound to the C-domain	Homo sapiens

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Release 2023.1 (January 2023)