Structure of PDB 1p18 Chain B

Receptor sequence
>1p18B (length=194) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
YEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLRGS
FMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEG
HHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQ
3D structure
PDB1p18 Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E111 D112 D115 F164 R177
Catalytic site (residue number reindexed from 1) E107 D108 D111 F160 R173
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 7HP B Y82 D115 K143 F164 V165 L170 Y78 D111 K139 F160 V161 L166
BS02 PRP B R52 S81 Y82 E111 D112 I113 D115 T116 A117 T119 R177 R48 S77 Y78 E107 D108 I109 D111 T112 A113 T115 R173
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

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Cellular Component
External links
PDB RCSB:1p18, PDBe:1p18, PDBj:1p18
PDBsum1p18
PubMed14698288
UniProtQ4DRC4

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