Structure of PDB 4v0x Chain A Binding Site BS01

Receptor Information
>4v0x Chain A (length=293) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLNIDSIIQRLLEVRGSGKNVQLQENEIRGLCLKSREIFLSQPILLELEA
PLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLL
LAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFN
CLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWS
DPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEF
FAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
Ligand information
>4v0x Chain B (length=24) Species: 9606 (Homo sapiens) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
KKVTFLEEVTEYYISGDEDRKGPW
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4v0x G-actin provides substrate-specificity to eukaryotic initiation factor 2 alpha holophosphatases.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		D71 R74 Y78 R96 G135 D242 F257 P270 C273 E287 L289 M290 C291 S292 F293 Q294 I295 K297 P298 A299
Binding residue
(residue number reindexed from 1)		D64 R67 Y71 R89 G128 D235 F250 P263 C266 E280 L282 M283 C284 S285 F286 Q287 I288 K290 P291 A292
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) D57 H59 D85 D88 R89 N117 H118 H166 R214 H241
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:4v0x, PDBe:4v0x, PDBj:4v0x
PDBsum4v0x
PubMed25774600
UniProtP63087|PP1G_MOUSE Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (Gene Name=Ppp1cc)

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