Structure of PDB 1qk4 Chain D

Receptor sequence
>1qk4D (length=219) Species: 383379 (Toxoplasma gondii RH) [Search protein sequence]
MASKPIEDYGKGKGRIEPMYIPDNTFYNADDFLVPPHCKPYIDKILLPGG
LVKDRVEKLAYDIHRTYFGEELHIICILKGSRGFFNLLIDYLATIQKYSG
RESSVPPFFEHYVRLKQLTVLSDDLSIFRDKHVLIVEDIVDTGFTLTEFG
ERLKAVGPKSMRIATLVEKRTDNSLKGDFVGFSIEDVWIVGCCYDFNEMF
RDFDHVAVLSDAARKKFEK
3D structure
PDB1qk4 Crystal Structures of the Toxoplasma Gondii Hypoxanthine-Guanine Phosphoribosyltransferase Gmp and -Imp Complexes: Comparison of Purine Binding Interactions with the Xmp Complex
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E146 D147 D150 W199 R212
Catalytic site (residue number reindexed from 1) E137 D138 D141 W188 R201
Enzyme Commision number 2.4.2.22: xanthine phosphoribosyltransferase.
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 IMP D E146 D147 I148 D150 T151 G152 T154 K178 W199 I200 E137 D138 I139 D141 T142 G143 T145 K169 W188 I189 MOAD: Kd=61uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0000310 xanthine phosphoribosyltransferase activity
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:0032265 XMP salvage
GO:0046100 hypoxanthine metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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External links
PDB RCSB:1qk4, PDBe:1qk4, PDBj:1qk4
PDBsum1qk4
PubMed10545170
UniProtQ26997|HGXR_TOXGO Hypoxanthine-guanine-xanthine phosphoribosyltransferase (Gene Name=HPRT)

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