Structure of PDB 1i0l Chain B

Receptor sequence
>1i0lB (length=194) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
YEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGS
FMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEG
HHVLIVEDIVNTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSAD
YVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARG
3D structure
PDB1i0l The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography.
ChainB
Resolution1.72 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E111 D112 N115 F164 R177
Catalytic site (residue number reindexed from 1) E107 D108 N111 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 B Y82 K143 F164 V165 Y78 K139 F160 V161
BS02 PRP B K52 G53 S81 Y82 E111 D112 I113 N115 T116 A117 T119 R177 K48 G49 S77 Y78 E107 D108 I109 N111 T112 A113 T115 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1i0l, PDBe:1i0l, PDBj:1i0l
PDBsum1i0l
PubMed11258886
UniProtQ4DRC4

[Back to BioLiP]