Structure of PDB 5by0 Chain A Binding Site BS01

Receptor Information
>5by0 Chain A (length=465) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GHMTIPGRFMTIDKGTFGEYTASTRWPIIIQNAIDDLSKHQETEKSNGTK
FEQGEVIKKELKEFRQEIIDRVPLRPFTEEEIKIANVPLSFNEYLKKHPE
VNWGAVEWLFSEVYLYRRVNVLFQRQCEWAKFDIFNRLKQSTFESSFYGV
VELALRYENLLPQLREMKQNDDILKVLFKEFIEISLWGNATDLSLLTNAT
LEDIKSIQGAKARAASESKIVVNDTEKAWEVLTKARADANSREIRVDFVL
DNSGFELYADLMLAAFLLQSGLATKCIFHAKDIPYMVSDVMLKDFDILVH
DLRDREFFPSGEPSTKESRALDLFAGEMEKFVSSGKIEFREDSFWTTELD
YWNLDANETKYHGSILHKDLQKSNLVIFKGDLNYRKLTGDRKWPRTTKWE
TAIGPLATNGITSLSLRTCKADVQVALPEGLDAKLSQEWEKENPGRGSWW
CCSGKWAVICFCSGI
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 chain5by0 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5by0 Crystal structure of magnesium-bound Duf89 protein Saccharomyces cerevisiae
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D254 N255 D292
Binding residue
(residue number reindexed from 1)		D251 N252 D289
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.-
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0046872 metal ion binding
GO:0097023 fructose 6-phosphate aldolase activity
GO:0103026 fructose-1-phosphatase activity
Biological Process
GO:0006974 DNA damage response
GO:0008150 biological_process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5by0, PDBe:5by0, PDBj:5by0
PDBsum5by0
PubMed
UniProtQ04371|ARMT1_YEAST Damage-control phosphatase YMR027W (Gene Name=YMR027W)

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