Structure of PDB 1wvc Chain A Binding Site BS01

Receptor Information
>1wvc Chain A (length=254) Species: 220341 (Salmonella enterica subsp. enterica serovar Typhi str. CT18) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASKAVILAGGLGTRLSEETIVKPKPMVEIGGKPILWHIMKMYSVHGIKDF
IICCGYKGYVIKEYFANYFLHMSDVTFHMAENRMEVHHKRVEPWNVTLVD
TGDSSMTGGRLKRVAEYVKDDEAFLFTYGDGVADLDIKATIDFHKAHGKK
ATLTATFPPGRGALDIQAGQVRSFQKGDGAMINGGFFVLNPSVIDLIDND
ATTWEQEPLMTLAQQGELMAFEHPGFWQPMDTLRDKVYLEGLWEKGKAPW
KTWE
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 chain1wvc Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1wvc Kinetic and structural analysis of alpha-D-Glucose-1-phosphate cytidylyltransferase from Salmonella typhi.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D131 D236
Binding residue
(residue number reindexed from 1)		D130 D231
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.7.33: glucose-1-phosphate cytidylyltransferase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0047343 glucose-1-phosphate cytidylyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009243 O antigen biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1wvc, PDBe:1wvc, PDBj:1wvc
PDBsum1wvc
PubMed15634670
UniProtQ8Z5I4|RFBF_SALTI Glucose-1-phosphate cytidylyltransferase (Gene Name=rfbF)

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