Structure of PDB 1a6q Chain A Binding Site BS01

Receptor Information
>1a6q Chain A (length=363) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLE
SWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGI
RTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLL
CRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFD
YKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELC
DFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEA
VKKEAELDKYLECRVEEIIKGVPDLVHVMRTLASENIPSLPPGGELASKR
NVIEAVYNRLNPY
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1a6q Chain A Residue 383 [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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PDB1a6q Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D60 D239 D282
Binding residue
(residue number reindexed from 1)		D59 D238 D281
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004721 phosphoprotein phosphatase activity
GO:0004722 protein serine/threonine phosphatase activity
GO:0005515 protein binding
GO:0017018 myosin phosphatase activity
GO:0030145 manganese ion binding
GO:0033192 calmodulin-dependent protein phosphatase activity
GO:0043169 cation binding
GO:0046872 metal ion binding
GO:0070412 R-SMAD binding
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0006470 protein dephosphorylation
GO:0006499 N-terminal protein myristoylation
GO:0006611 protein export from nucleus
GO:0016311 dephosphorylation
GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
GO:0030514 negative regulation of BMP signaling pathway
GO:0035970 peptidyl-threonine dephosphorylation
GO:0043123 positive regulation of canonical NF-kappaB signal transduction
GO:0043124 negative regulation of canonical NF-kappaB signal transduction
GO:0045893 positive regulation of DNA-templated transcription
GO:0046827 positive regulation of protein export from nucleus
GO:0051726 regulation of cell cycle
GO:0071560 cellular response to transforming growth factor beta stimulus
GO:0090263 positive regulation of canonical Wnt signaling pathway
GO:1901223 negative regulation of non-canonical NF-kappaB signal transduction
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1a6q, PDBe:1a6q, PDBj:1a6q
PDBsum1a6q
PubMed9003755
UniProtP35813|PPM1A_HUMAN Protein phosphatase 1A (Gene Name=PPM1A)

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