Structure of PDB 1yfz Chain B Binding Site BS01

Receptor Information
>1yfz Chain B (length=177) Species: 273068 (Caldanaerobacter subterraneus subsp. tengcongensis MB4) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PMEDIEEILITEEQLKAKVKELGEMITRDYEGKDLVLIGVLKGAIMFMSG
LSRAIDLPLSIDFLAVSSYGSSTKSSGIVKIIKDHDIDIEGKDVLIVEDI
IDSGLTLAYLRETLLGRKPRSLKICTILDKPERREADVKVDYCGFKIPDK
FVVGYGLDYAEKYRNLPFIGVLKPELY
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1yfz Chain B Residue 2191 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1yfz Alternative IMP Binding in Feedback Inhibition of Hypoxanthine-Guanine Phosphoribosyltransferase from Thermoanaerobacter tengcongensis.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
E101 D102
Binding residue
(residue number reindexed from 1)
E98 D99
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E101 D102 D105 F154 R167
Catalytic site (residue number reindexed from 1) E98 D99 D102 F151 R164
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:1yfz, PDBe:1yfz, PDBj:1yfz
PDBsum1yfz
PubMed15854655
UniProtQ8R7L0

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