Structure of PDB 8omd Chain D

Receptor sequence
>8omdD (length=295) Species: 10090 (Mus musculus) [Search protein sequence]
KQILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLL
GARCAFMGSLAPGHVADFLVADFRQRGVDVSQVTWQSQGDTPCSCCIVNN
SNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRI
EEHNAKQPLPQKVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQS
AVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDAFPPPRVVDT
LGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQGFDGIV
3D structure
PDB8omd Crystal structures of human and mouse ketohexokinase provide a structural basis for species- and isoform-selective inhibitor design.
ChainD
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.3: ketohexokinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 VTJ D N105 S107 A226 V250 A256 G257 F260 A285 C289 N102 S104 A223 V247 A253 G254 F257 A282 C286
Gene Ontology
Molecular Function
GO:0004454 ketohexokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
Biological Process
GO:0006000 fructose metabolic process
GO:0006001 fructose catabolic process
GO:0006796 phosphate-containing compound metabolic process
GO:0016310 phosphorylation
GO:0046835 carbohydrate phosphorylation
GO:0061624 fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate
GO:0061625 glycolytic process through fructose-1-phosphate
GO:0070873 regulation of glycogen metabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8omd, PDBe:8omd, PDBj:8omd
PDBsum8omd
PubMed37712434
UniProtP97328|KHK_MOUSE Ketohexokinase (Gene Name=Khk)

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