Structure of PDB 4lac Chain C Binding Site BS02

Receptor Information
>4lac Chain C (length=290) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVT
VCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVAL
KVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYL
PLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDP
DDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHD
RNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAP
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 chain4lac Chain C Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4lac Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone.
Resolution2.82 Å
Binding residue
(original residue number in PDB)		D57 H59 D85
Binding residue
(residue number reindexed from 1)		D54 H56 D82
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D57 H59 D85 D88 R89 N117 H118 H167 R214 H241
Catalytic site (residue number reindexed from 1) D54 H56 D82 D85 R86 N114 H115 H164 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:0004725 protein tyrosine phosphatase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0017018 myosin phosphatase activity
GO:0046872 metal ion binding
GO:0046982 protein heterodimerization activity
GO:0048156 tau protein binding
GO:0050811 GABA receptor binding
Biological Process
GO:0000278 mitotic cell cycle
GO:0001932 regulation of protein phosphorylation
GO:0006470 protein dephosphorylation
GO:0007498 mesoderm development
GO:0010288 response to lead ion
GO:0010719 negative regulation of epithelial to mesenchymal transition
GO:0035331 negative regulation of hippo signaling
GO:0035556 intracellular signal transduction
GO:0035970 peptidyl-threonine dephosphorylation
GO:0040008 regulation of growth
GO:0043029 T cell homeostasis
GO:0045595 regulation of cell differentiation
GO:0051321 meiotic cell cycle
GO:0051898 negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO:0070262 peptidyl-serine dephosphorylation
GO:0071902 positive regulation of protein serine/threonine kinase activity
GO:1900227 positive regulation of NLRP3 inflammasome complex assembly
GO:1904526 regulation of microtubule binding
GO:1904528 positive regulation of microtubule binding
GO:1904539 negative regulation of glycolytic process through fructose-6-phosphate
GO:2000045 regulation of G1/S transition of mitotic cell cycle
Cellular Component
GO:0000159 protein phosphatase type 2A complex
GO:0000775 chromosome, centromeric region
GO:0000922 spindle pole
GO:0005634 nucleus
GO:0005694 chromosome
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0008287 protein serine/threonine phosphatase complex
GO:0015630 microtubule cytoskeleton
GO:0016020 membrane
GO:0045121 membrane raft
GO:0045202 synapse
GO:0070062 extracellular exosome
GO:0090443 FAR/SIN/STRIPAK complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4lac, PDBe:4lac, PDBj:4lac
PDBsum4lac
PubMed24100351
UniProtP67775|PP2AA_HUMAN Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (Gene Name=PPP2CA)

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