Structure of PDB 1p17 Chain C

Receptor sequence
>1p17C (length=192) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
PREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVL
RGSFMFTADLCRALCDFNVPVRMEFICVSSYGESSGQVRMLLDTRHSIEG
HHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAA
3D structure
PDB1p17 Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 IMP C I113 D115 T116 A117 K143 F164 V165 I109 D111 T112 A113 K139 F160 V161
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1p17, PDBe:1p17, PDBj:1p17
PDBsum1p17
PubMed14698288
UniProtQ4DRC4

[Back to BioLiP]