Structure of PDB 4i5n Chain F Binding Site BS03

Receptor Information

>4i5n Chain F (length=294) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

EKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPV
TVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVA
LKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDY
LPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSD
PDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCH
DRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRG

Ligand information

Ligand ID

InChI

InChI=1S/Mn/q+2

InChIKey

WAEMQWOKJMHJLA-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mn+2]
CACTVS 3.341	[Mn++]

Formula

Name

MANGANESE (II) ION

PDB chain

4i5n Chain F Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	4i5n Structure of the Ca(2+)-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation.
Resolution	2.8 Å
Binding residue (original residue number in PDB)	D57 H59 D85 H167
Binding residue (residue number reindexed from 1)	D55 H57 D83 H165
Annotation score	1

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)	D55 H57 D83 D86 R87 N115 H116 H165 R212 H239
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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Cellular Component

External links

PDB	RCSB:4i5n, PDBe:4i5n, PDBj:4i5n
PDBsum	4i5n
PubMed	23752926
UniProt	P67775\|PP2AA_HUMAN Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (Gene Name=PPP2CA)

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