Structure of PDB 5zqv Chain D Binding Site BS01

Receptor Information
>5zqv Chain D (length=294) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLEL
EAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETIC
LLLAYKIRYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDC
FNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLL
WSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGY
EFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA
Ligand information
>5zqv Chain G (length=20) Species: 9606 (Homo sapiens) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
RRVSFADSFGFNLVSVKEFD
Receptor-Ligand Complex Structure
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PDB5zqv Structural basis for protein phosphatase 1 recruitment by glycogen-targeting subunits.
Resolution2.95 Å
Binding residue
(original residue number in PDB)		R74 Y78 K168 D242 Y255 F257 R261 E287 L289 M290 C291 F293 I295 L296 K297 P298 A299
Binding residue
(residue number reindexed from 1)		R69 Y73 K163 D237 Y250 F252 R256 E282 L284 M285 C286 F288 I290 L291 K292 P293 A294
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:0006417 regulation of translation
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:0045725 positive regulation of glycogen biosynthetic process
GO:0048511 rhythmic process
GO:0048754 branching morphogenesis of an epithelial tube
GO:0051301 cell division
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: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:5zqv, PDBe:5zqv, PDBj:5zqv
PDBsum5zqv
PubMed30422398
UniProtP62137|PP1A_MOUSE Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=Ppp1ca)

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