Structure of PDB 1jee Chain A Binding Site BS01

Receptor Information
>1jee Chain A (length=510) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNG
GFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTR
IALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGD
YYVGGSLEAIQLPQHYDYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMH
RAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPN
GIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKG
VDFYGPYDAQELVESYKHELDIEVVPFRMVTYLPDEDRYAPIDQIDTTKT
RTLNISGTELRRRLRVGGEIPEWFSYPEVVKILRESNPPRPKQGFSIVLG
NSLTVSREQLSIALLSTFLQFGGGRYYKIFEHNNKTELLSLIQDFIGSGS
GLIIPNQWEDDKDSVVGKQNVYLLDTSSSADIQLESADEPISHIVQKVVL
FLEDNGFFVF
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 chain1jee Chain A Residue 521 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1jee The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		E46 P164 H166
Binding residue
(residue number reindexed from 1)		E45 P163 H165
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T196 R197 H201 H204 R290
Catalytic site (residue number reindexed from 1) T195 R196 H200 H203 R289
Enzyme Commision number 2.7.7.4: sulfate adenylyltransferase.
Gene Ontology
Molecular Function
GO:0004781 sulfate adenylyltransferase (ATP) activity
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0000096 sulfur amino acid metabolic process
GO:0000103 sulfate assimilation
GO:0006790 sulfur compound metabolic process
GO:0010134 sulfate assimilation via adenylyl sulfate reduction
GO:0019379 sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
GO:0070814 hydrogen sulfide biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jee, PDBe:1jee, PDBj:1jee
PDBsum1jee
PubMed11700067
UniProtP08536|MET3_YEAST Sulfate adenylyltransferase (Gene Name=MET3)

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