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ATP bind site of phospho- glycerate kinase

ATP bind site of phospho- glycerate kinase

A605/0033

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Credit

OXFORD MOLECULAR BIOPHYSICS LABORATORY / SCIENCE PHOTO LIBRARY OXFORD MOLECULAR BIOPHYSICS LABORATORY / SCIENCE PHOTO LIBRARY

Caption

Computer graphics representation of the ATP- binding domain (reaction site) of phosphoglycerate kinase, a glycolytic enzyme (catalyst). In glycolysis, glucose is converted to pyruvate with the production of ATP: in other words, a catabolic reaction provides metabolic energy (as ATP) at the expense of the degradation of food molecules (glucose). This crystal structure is of horse phosphoglycerate kinase, a bi-lobed structure composed of two domains (one for each reactant), each composed of a six-stranded beta sheet surrounded by alpha helices (blue ribbons). Here, Van der Waals bonded ATP appears in red. This enzyme catalyses the transfer of a phosphoryl group from 1,3-diphosphoglyerate to ADP to yield ATP & 3- phosphoglycerate. Proposed mechanism involves hinge- bending to unite substrates.

Release details

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