Structure of PDB 1p17 Chain B

Receptor sequence
>1p17B (length=204) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
PREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVL
RGSFMFTADLCRALCDFNVPVRMEFICVSSYSGQVRMLLDTRHSIEGHHV
LIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSADYVV
ANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQKKQRAIGSA
DTDR
3D structure
PDB1p17 Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase.
ChainB
Resolution2.7 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) E104 D105 D108 F157 R170
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 IMP B D112 I113 D115 T116 A117 T119 K143 F164 V165 D105 I106 D108 T109 A110 T112 K136 F157 V158
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:1p17, PDBe:1p17, PDBj:1p17
PDBsum1p17
PubMed14698288
UniProtQ4DRC4

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