Structure of PDB 3juk Chain D Binding Site BS02

Receptor Information
>3juk Chain D (length=264) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIKKCLFPAAGYGTRFLPITKTIPKEMLPIVDKPLIQYAVEEAMEAGCEV
MAIVTGRNKRSLEDYFDTSYTNKENALKSIRNIIEKCCFSYVRQKQMKGL
GHAILTGEALIGNEPFAVILADDLCISHDHPSVLKQMTSLYQKYQCSIVA
IEEVALEEVSKYGVIRGEWLEEGVYEIKDMVEKPNQEDAPSNLAVIGRYI
LTPDIFEILSETKPGKNNEIQITDALRTQAKRKRIIAYQFKGKRYDCGSV
EGYIEASNAYYKKR
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 chain3juk Chain D Residue 311 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3juk Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase
Resolution2.3 Å
Binding residue
(original residue number in PDB)		T14 R15
Binding residue
(residue number reindexed from 1)		T14 R15
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.7.9: UTP--glucose-1-phosphate uridylyltransferase.
Gene Ontology
Molecular Function
GO:0003983 UTP:glucose-1-phosphate uridylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006011 UDP-glucose metabolic process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3juk, PDBe:3juk, PDBj:3juk
PDBsum3juk
PubMed20238176
UniProtO25363

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