Structure of PDB 1i0i Chain A

Receptor sequence
>1i0iA (length=187) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
YEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGS
FMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEG
HHVLIVEDIVQTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYA
3D structure
PDB1i0i The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography.
ChainA
Resolution2.06 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 Q115 F164 R177
Catalytic site (residue number reindexed from 1) E107 D108 Q111 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 K143 F164 V165 K139 F160 V161
BS02 PRP A K52 G53 E111 D112 I113 V114 Q115 T116 R177 K48 G49 E107 D108 I109 V110 Q111 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

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Cellular Component
External links
PDB RCSB:1i0i, PDBe:1i0i, PDBj:1i0i
PDBsum1i0i
PubMed11258886
UniProtQ4DRC4

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