Structure of PDB 1p17 Chain A

Receptor sequence

>1p17A (length=194) Species: 5693 (Trypanosoma cruzi)

PREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVL
RGSFMFTADLCRALCDFNVPVRMEFICVSSYGTSSGQVRMLLDTRHSIEG
HHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQ

3D structure

• PDB: 1p17 Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase.
• Chain: A
• Resolution: 2.7 Å

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	A	E111 D112 I113 V114 D115 T116 A117 T119 F164	E107 D108 I109 V110 D111 T112 A113 T115 F160	PDBbind-CN: -logKd/Ki=2.82,Kd=1.5mM

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

External links

• PDB: RCSB:1p17, PDBe:1p17, PDBj:1p17
• PDBsum: 1p17
• PubMed: 14698288
• UniProt: Q4DRC4