Structure of PDB 5jsq Chain A

Receptor sequence
>5jsqA (length=173) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
CKYDFATSVLFTEAELHTRMRGVAQRIADDYSNCNLKPLENPLVIVSVLK
GSFVFTADMVRILGDFGVPTRVEFLRDIRGKHVLVLEDILDTALTLREVV
DSLKKSEPASIKTLVAIDKPGGRKIPFTAEYVVADVPNVFVVGYGLDYDQ
SYREVRDVVILKPSVYETWGKEL
3D structure
PDB5jsq Crystal structures and inhibition of Trypanosoma brucei hypoxanthine-guanine phosphoribosyltransferase.
ChainA
Resolution1.503 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E113 D114 D117 F166 R179
Catalytic site (residue number reindexed from 1) E87 D88 D91 F140 R153
Enzyme Commision number 2.4.2.8: hypoxanthine phosphoribosyltransferase.
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 6MS A L53 E113 I115 D117 T118 A119 T121 K145 F166 V167 D173 L49 E87 I89 D91 T92 A93 T95 K119 F140 V141 D147 MOAD: Ki=21.3uM
PDBbind-CN: -logKd/Ki=4.67,Ki=21.3uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004422 hypoxanthine phosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0046872 metal ion binding
GO:0052657 guanine phosphoribosyltransferase activity
Biological Process
GO:0006166 purine ribonucleoside salvage
GO:0006178 guanine salvage
GO:0032263 GMP salvage
GO:0032264 IMP salvage
GO:0046100 hypoxanthine metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0020015 glycosome
GO:0031981 nuclear lumen
GO:0097014 ciliary plasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:5jsq, PDBe:5jsq, PDBj:5jsq
PDBsum5jsq
PubMed27786284
UniProtQ07010|HPRT_TRYBB Hypoxanthine-guanine phosphoribosyltransferase (Gene Name=HGPRT)

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