Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LAC

Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A phosphatase activator (PTPA) complex with ATPgammaS

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0019211	molecular_function	phosphatase activator activity
C	0000159	cellular_component	protein phosphatase type 2A complex
C	0000278	biological_process	mitotic cell cycle
C	0000775	cellular_component	chromosome, centromeric region
C	0000785	cellular_component	chromatin
C	0000922	cellular_component	spindle pole
C	0004721	molecular_function	phosphoprotein phosphatase activity
C	0004722	molecular_function	protein serine/threonine phosphatase activity
C	0004725	molecular_function	protein tyrosine phosphatase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0005856	cellular_component	cytoskeleton
C	0005886	cellular_component	plasma membrane
C	0006357	biological_process	regulation of transcription by RNA polymerase II
C	0006366	biological_process	transcription by RNA polymerase II
C	0006368	biological_process	transcription elongation by RNA polymerase II
C	0006470	biological_process	protein dephosphorylation
C	0007498	biological_process	mesoderm development
C	0008287	cellular_component	protein serine/threonine phosphatase complex
C	0010288	biological_process	response to lead ion
C	0010719	biological_process	negative regulation of epithelial to mesenchymal transition
C	0015630	cellular_component	microtubule cytoskeleton
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0031113	biological_process	regulation of microtubule polymerization
C	0035331	biological_process	negative regulation of hippo signaling
C	0035556	biological_process	intracellular signal transduction
C	0035970	biological_process	peptidyl-threonine dephosphorylation
C	0040008	biological_process	regulation of growth
C	0043029	biological_process	T cell homeostasis
C	0045121	cellular_component	membrane raft
C	0045202	cellular_component	synapse
C	0045595	biological_process	regulation of cell differentiation
C	0046872	molecular_function	metal ion binding
C	0046982	molecular_function	protein heterodimerization activity
C	0048156	molecular_function	tau protein binding
C	0050811	molecular_function	GABA receptor binding
C	0051321	biological_process	meiotic cell cycle
C	0051898	biological_process	negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
C	0070062	cellular_component	extracellular exosome
C	0090090	biological_process	negative regulation of canonical Wnt signaling pathway
C	0090443	cellular_component	FAR/SIN/STRIPAK complex
C	0097706	biological_process	vascular endothelial cell response to oscillatory fluid shear stress
C	0160232	cellular_component	INTAC complex
C	0160240	biological_process	RNA polymerase II transcription initiation surveillance
C	0180006	molecular_function	RNA polymerase II CTD heptapeptide repeat S2 phosphatase activity
C	0180007	molecular_function	RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
C	0180008	molecular_function	RNA polymerase II CTD heptapeptide repeat S7 phosphatase activity
C	1900227	biological_process	positive regulation of NLRP3 inflammasome complex assembly
C	1904539	biological_process	negative regulation of glycolytic process through fructose-6-phosphate
C	2000045	biological_process	regulation of G1/S transition of mitotic cell cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG A 601

Chain	Residue
A	ALA415
A	LYS416
A	TRP417
A	ARG420
A	HOH716
A	HOH719
C	ASP290

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN C 501

Chain	Residue
C	HIS167
C	HIS241
C	MN502
C	AGS503
C	ASP85
C	ASN117

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 502

Chain	Residue
C	ASP57
C	HIS59
C	ASP85
C	MN501
C	AGS503

site_id	AC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE AGS C 503

Chain	Residue
B	ARG148
B	ASP150
B	GLY152
B	THR153
B	GLY154
B	PRO203
B	ALA204
B	GLY205
B	PRO304
B	VAL305
B	GLN307
B	HIS308
C	ASP57
C	HIS59
C	ASP85
C	ARG89
C	ASN117
C	HIS118
C	TYR127
C	ARG214
C	HIS241
C	MN501
C	MN502
C	HOH604
C	HOH656

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MES C 504

Chain	Residue
C	GLN61
C	PHE62
C	HIS63
C	ASP64
C	PRO263
C	ASN264
C	TYR267
C	PRO291

Functional Information from PROSITE/UniProt

site_id	PS00125
Number of Residues	6
Details	SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE

Chain	Residue	Details
C	LEU114-GLU119

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250\|UniProtKB:P36873

Chain	Residue	Details
C	HIS118
B	TYR188
B	LEU189

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:38123684, ECO:0007744\|PDB:8SO0, ECO:0007744\|PDB:8TTB

Chain	Residue	Details
C	ASP57
C	HIS59
C	ASP85

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:17055435, ECO:0000269\|PubMed:33243860, ECO:0000269\|PubMed:33633399, ECO:0000269\|PubMed:34762484, ECO:0007744\|PDB:7CUN, ECO:0007744\|PDB:7K36, ECO:0007744\|PDB:7PKS

Chain	Residue	Details
C	ASN117
C	HIS167
C	HIS241

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P67774

Chain	Residue	Details
C	TYR307

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Leucine methyl ester => ECO:0000269\|PubMed:38123684, ECO:0000269\|PubMed:8206937, ECO:0007744\|PDB:8SO0, ECO:0007744\|PDB:8TTB

Chain	Residue	Details
C	LEU309

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)