Structure of PDB 1i13 Chain A

Receptor sequence

>1i13A (length=187) Species: 5693 (Trypanosoma cruzi)

YEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGS
FMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEG
HHVLIVEDIVATALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYA

3D structure

• PDB: 1i13 The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography.
• Chain: A
• Resolution: 1.84 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E111 D112 A115 F164 R177
• Catalytic site (residue number reindexed from 1): E107 D108 A111 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	A	I113 K143 F164 V165	I109 K139 F160 V161
BS02	PRP	A	K52 G53 D112 I113 A115 T116 R177	K48 G49 D108 I109 A111 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:1i13, PDBe:1i13, PDBj:1i13
• PDBsum: 1i13
• PubMed: 11258886
• UniProt: Q4DRC4