Structure of PDB 1i0i Chain A Binding Site BS02

Receptor Information
>1i0i Chain A (length=187) Species: 5693 (Trypanosoma cruzi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGS
FMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEG
HHVLIVEDIVQTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYA
Ligand information
Ligand IDPRP
InChIInChI=1S/C5H13O14P3/c6-3-2(1-16-20(8,9)10)17-5(4(3)7)18-22(14,15)19-21(11,12)13/h2-7H,1H2,(H,14,15)(H2,8,9,10)(H2,11,12,13)/t2-,3-,4-,5-/m1/s1
InChIKeyPQGCEDQWHSBAJP-TXICZTDVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)OP(=O)(O)OP(=O)(O)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@H]([C@H](O1)O[P@@](=O)(O)OP(=O)(O)O)O)O)OP(=O)(O)O
CACTVS 3.341O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(O)=O)O[P](O)(=O)O[P](O)(O)=O
ACDLabs 10.04O=P(OC1OC(C(O)C1O)COP(=O)(O)O)(O)OP(=O)(O)O
CACTVS 3.341O[C@H]1[C@@H](O)[C@H](O[C@@H]1CO[P](O)(O)=O)O[P@](O)(=O)O[P](O)(O)=O
FormulaC5 H13 O14 P3
Name1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose;
ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC ACID;
1-O-pyrophosphono-5-O-phosphono-alpha-D-ribose;
1-O-pyrophosphono-5-O-phosphono-D-ribose;
1-O-pyrophosphono-5-O-phosphono-ribose
ChEMBL
DrugBankDB01632
ZINCZINC000008215630
PDB chain1i0i Chain A Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1i0i The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography.
Resolution2.06 Å
Binding residue
(original residue number in PDB)		K52 G53 E111 D112 I113 V114 Q115 T116 R177
Binding residue
(residue number reindexed from 1)		K48 G49 E107 D108 I109 V110 Q111 T112 R173
Annotation score5
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.
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1i0i, PDBe:1i0i, PDBj:1i0i
PDBsum1i0i
PubMed11258886
UniProtQ4DRC4

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