Structure of PDB 6obp Chain A Binding Site BS01

Receptor Information
>6obp Chain A (length=298) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQP
ILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQS
LETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWK
TFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGL
LCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQV
VEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP
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 chain6obp Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6obp SDS22 selectively recognizes and traps metal-deficient inactive PP1.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		D92 N124 H173 H248
Binding residue
(residue number reindexed from 1)		D92 N124 H173 H248
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0004721 phosphoprotein phosphatase activity
GO:0004722 protein serine/threonine phosphatase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008157 protein phosphatase 1 binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0017018 myosin phosphatase activity
GO:0043021 ribonucleoprotein complex binding
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0098641 cadherin binding involved in cell-cell adhesion
Biological Process
GO:0005977 glycogen metabolic process
GO:0005979 regulation of glycogen biosynthetic process
GO:0005981 regulation of glycogen catabolic process
GO:0006470 protein dephosphorylation
GO:0010288 response to lead ion
GO:0016311 dephosphorylation
GO:0030324 lung development
GO:0032922 circadian regulation of gene expression
GO:0042752 regulation of circadian rhythm
GO:0043153 entrainment of circadian clock by photoperiod
GO:0043247 telomere maintenance in response to DNA damage
GO:0043558 regulation of translational initiation in response to stress
GO:0045725 positive regulation of glycogen biosynthetic process
GO:0048754 branching morphogenesis of an epithelial tube
GO:0051301 cell division
GO:0060828 regulation of canonical Wnt signaling pathway
GO:0098609 cell-cell adhesion
GO:2001241 positive regulation of extrinsic apoptotic signaling pathway in absence of ligand
Cellular Component
GO:0000164 protein phosphatase type 1 complex
GO:0000781 chromosome, telomeric region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005912 adherens junction
GO:0042587 glycogen granule
GO:0043025 neuronal cell body
GO:0043197 dendritic spine
GO:0043204 perikaryon
GO:0070062 extracellular exosome
GO:0072357 PTW/PP1 phosphatase complex
GO:0098793 presynapse
GO:0098794 postsynapse
GO:0098978 glutamatergic synapse

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6obp, PDBe:6obp, PDBj:6obp
PDBsum6obp
PubMed31548429
UniProtP62136|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

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