Structure of PDB 4v0v Chain C Binding Site BS02

Receptor Information
>4v0v Chain C (length=290) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLNIDSIIQRLLEVRGNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAY
KIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLP
IAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPD
KDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAK
RQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
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 chain4v0v Chain C Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4v0v G-actin provides substrate-specificity to eukaryotic initiation factor 2 alpha holophosphatases.
Resolution1.61 Å
Binding residue
(original residue number in PDB)		D92 N124 H173 H248
Binding residue
(residue number reindexed from 1)		D82 N114 H163 H238
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D64 H66 D92 D95 R96 N124 H125 H173 R221 H248
Catalytic site (residue number reindexed from 1) D54 H56 D82 D85 R86 N114 H115 H163 R211 H238
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:0005515 protein binding
GO:0005521 lamin binding
GO:0008157 protein phosphatase 1 binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0017018 myosin phosphatase activity
GO:0019901 protein kinase binding
GO:0019903 protein phosphatase binding
GO:0019904 protein domain specific binding
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
Biological Process
GO:0001824 blastocyst development
GO:0005977 glycogen metabolic process
GO:0006470 protein dephosphorylation
GO:0007283 spermatogenesis
GO:0030182 neuron differentiation
GO:0032922 circadian regulation of gene expression
GO:0042752 regulation of circadian rhythm
GO:0043153 entrainment of circadian clock by photoperiod
GO:0046822 regulation of nucleocytoplasmic transport
GO:0048511 rhythmic process
GO:0051301 cell division
GO:0060252 positive regulation of glial cell proliferation
Cellular Component
GO:0000775 chromosome, centromeric region
GO:0000776 kinetochore
GO:0000781 chromosome, telomeric region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005694 chromosome
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005741 mitochondrial outer membrane
GO:0005815 microtubule organizing center
GO:0005856 cytoskeleton
GO:0016607 nuclear speck
GO:0030496 midbody
GO:0032154 cleavage furrow
GO:0032991 protein-containing complex
GO:0043197 dendritic spine
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:4v0v, PDBe:4v0v, PDBj:4v0v
PDBsum4v0v
PubMed25774600
UniProtP63087|PP1G_MOUSE Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (Gene Name=Ppp1cc)

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