Structure of PDB 1p18 Chain A

Receptor sequence

>1p18A (length=187) Species: 5693 (Trypanosoma cruzi)

YEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLRGS
FMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEG
HHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYA

3D structure

• PDB: 1p18 Interactions at the dimer interface influence the relative efficiencies for purine nucleotide synthesis and pyrophosphorolysis in a phosphoribosyltransferase
• Chain: A
• Resolution: 2.0 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	MG	A	E111 D112	E107 D108
BS02	7HP	A	K143 F164 V165 L170	K139 F160 V161 L166
BS03	PRP	A	R52 G53 E111 D112 I113 D115 T116 R177	R48 G49 E107 D108 I109 D111 T112 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

External links

• PDB: RCSB:1p18, PDBe:1p18, PDBj:1p18
• PDBsum: 1p18
• PubMed: 14698288
• UniProt: Q4DRC4