Structure of PDB 6zeh Chain B Binding Site BS03

Receptor Information
>6zeh Chain B (length=308) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPIL
LELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLE
TICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTF
TDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLC
DLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVE
DGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPQSAS
RENLLEEQ
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain6zeh Chain B Residue 503 [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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PDB6zeh Molecular basis for substrate specificity of the Phactr1/PP1 phosphatase holoenzyme.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		D92 N124 H125 R221 H248 A328 S329
Binding residue
(residue number reindexed from 1)		D90 N122 H123 R219 H246 A299 S300
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:6zeh, PDBe:6zeh, PDBj:6zeh
PDBsum6zeh
PubMed32975518
UniProtP62136|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA);
Q13813

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