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1QHA

HUMAN HEXOKINASE TYPE I COMPLEXED WITH ATP ANALOGUE AMP-PNP

Summary for 1QHA
Entry DOI10.2210/pdb1qha/pdb
DescriptorPROTEIN (HEXOKINASE), alpha-D-glucopyranose, 6-O-phosphono-alpha-D-glucopyranose, ... (6 entities in total)
Functional Keywordskinase, glycolysis, phosphotransferase, transferase
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight208167.50
Authors
Rosano, C.,Sabini, E.,Deriu, D.,Magnani, M.,Bolognesi, M. (deposition date: 1999-05-11, release date: 1999-11-10, Last modification date: 2023-08-16)
Primary citationRosano, C.,Sabini, E.,Rizzi, M.,Deriu, D.,Murshudov, G.,Bianchi, M.,Serafini, G.,Magnani, M.,Bolognesi, M.
Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control.
Structure Fold.Des., 7:1427-1437, 1999
Cited by
PubMed Abstract: 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 I is believed to optimize the ATP/ADP exchange between glucose phosphorylation and the mitochondrial oxidative phosphorylation reactions.
PubMed: 10574795
DOI: 10.1016/S0969-2126(00)80032-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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