Structure of PDB 4ja7 Chain A Binding Site BS01

Receptor Information
>4ja7 Chain A (length=466) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAY
LRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETV
VKVKPNDKDAKMKYQECSKIVKQKAFERSVVDSLDIESMTIEDEYSGPKL
EDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTL
KETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVE
VILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELF
SEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPM
CDLLWSDPQPQNGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKA
EGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPH
PNVKPMAYANTLLQLG
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 chain4ja7 Chain A Residue 501 [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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PDB4ja7 Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D271 N303 H352 H427
Binding residue
(residue number reindexed from 1)		D240 N272 H321 H396
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D242 H244 D271 D274 R275 N303 H304 H352 R400 H427
Catalytic site (residue number reindexed from 1) D211 H213 D240 D243 R244 N272 H273 H321 R369 H396
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0001965 G-protein alpha-subunit binding
GO:0003723 RNA binding
GO:0004721 phosphoprotein phosphatase activity
GO:0004722 protein serine/threonine phosphatase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008017 microtubule binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0017018 myosin phosphatase activity
GO:0031072 heat shock protein binding
GO:0042802 identical protein binding
GO:0043531 ADP binding
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
GO:0051879 Hsp90 protein binding
Biological Process
GO:0010288 response to lead ion
GO:0043066 negative regulation of apoptotic process
GO:0043278 response to morphine
GO:0070262 peptidyl-serine dephosphorylation
GO:0070301 cellular response to hydrogen peroxide
GO:0071276 cellular response to cadmium ion
GO:1904550 response to arachidonate
GO:2000324 positive regulation of glucocorticoid receptor signaling pathway
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0032991 protein-containing complex
GO:0043025 neuronal cell body
GO:0043204 perikaryon
GO:0101031 protein folding chaperone complex
GO:1990635 proximal dendrite

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4ja7, PDBe:4ja7, PDBj:4ja7
PDBsum4ja7
PubMed26182372
UniProtP53042|PPP5_RAT Serine/threonine-protein phosphatase 5 (Gene Name=Ppp5c)

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