Structure of PDB 1u2s Chain A Binding Site BS02

Receptor Information
>1u2s Chain A (length=244) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRQLLLISDLDNTWVGDQQALEHLQEYLGDRRGNFYLAYATGRSYHSARE
LQKQVGLMEPDYWLTAVGSEIYHPEGLDQHWADYLSEHWQRDILQAIADG
FEALKPQSPLEQNPWKISYHLDPQACPTVIDQLTEMLKETGIPVQVIFSS
GKDVDLLPQRSNKGNATQYLQQHLAMEPSQTLVCGDSGNDIGLFETSARG
VIVRNAQPELLHWYDQWGDSRHYRAQSSHAGAILEAIAHFDFLS
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 chain1u2s Chain A Residue 246 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1u2s The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D9 D186 S187 N189 D190
Binding residue
(residue number reindexed from 1)		D9 D186 S187 N189 D190
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.24: sucrose-phosphate phosphatase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0046872 metal ion binding
GO:0050307 sucrose-phosphate phosphatase activity
Biological Process
GO:0005986 sucrose biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1u2s, PDBe:1u2s, PDBj:1u2s
PDBsum1u2s
PubMed15937230
UniProtP74325

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