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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1bzy

E.C. namehypoxanthine phosphoribosyltransferase
SpeciesHomo sapiens (Human)
E.C. Number (IntEnz) 2.4.2.8
CSA Homologues of 1bzyThere are 46 Homologs
CSA Entries With UniProtID P00492
CSA Entries With EC Number 2.4.2.8
PDBe Entry 1bzy
PDBSum Entry 1bzy
MACiE Entry M0048

Literature Report

Introduction
Mechansim
Reaction

Catalytic Sites for 1bzy

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA133134macie:sideChain
AspA134135macie:sideChain
ArgA169170macie:sideChain
AspA137138macie:sideChain
TyrA104macie:sideChainStabilises the transition state by pi-cation interactions.

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluB133134macie:sideChain
AspB134135macie:sideChain
ArgB169170macie:sideChain
AspB137138macie:sideChain
TyrB104macie:sideChainStabilises the transition state by pi-cation interactions.

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluC133134macie:sideChain
AspC134135macie:sideChain
ArgC169170macie:sideChain
AspC137138macie:sideChain
TyrC104macie:sideChainStabilises the transition state by pi-cation interactions.

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluD133134macie:sideChain
AspD134135macie:sideChain
ArgD169170macie:sideChain
AspD137138macie:sideChain
TyrD104macie:sideChainStabilises the transition state by pi-cation interactions.

Literature References

Notes:
Shi W
The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor.
Nat Struct Biol 1999 6 588-593
PubMed: 10360366
Canyuk B
The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography.
Biochemistry 2001 40 2754-2765
PubMed: 11258886
Héroux A
Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: the structural basis for catalysis.
Structure 2000 8 1309-1318
PubMed: 11188695
Héroux A
Crystal structure of Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase with XMP, pyrophosphate, and two Mg(2+) ions bound: insights into the catalytic mechanism.
Biochemistry 1999 38 14495-14506
PubMed: 10545171
Jardim A
The conserved serine-tyrosine dipeptide in Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase is essential for catalytic activity.
J Biol Chem 1997 272 8967-8973
PubMed: 9083019
Xu Y
Catalysis in human hypoxanthine-guanine phosphoribosyltransferase: Asp 137 acts as a general acid/base.
Biochemistry 1998 37 4114-4124
PubMed: 9521733
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