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	0005886	cellular_component	plasma membrane
C	0006357	biological_process	regulation of transcription by RNA polymerase II
C	0006470	biological_process	protein dephosphorylation
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	0016180	biological_process	snRNA processing
C	0016787	molecular_function	hydrolase activity
C	0031113	biological_process	regulation of microtubule polymerization
C	0032039	cellular_component	integrator complex
C	0034243	biological_process	regulation of transcription elongation by RNA polymerase II
C	0035330	biological_process	regulation of hippo signaling
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	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16916641","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HV7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16916641","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HV6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	38
Details	Repeat: {"description":"HEAT 11","evidences":[{"source":"PubMed","id":"38123684","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SO0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8TTB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	38
Details	Repeat: {"description":"HEAT 12","evidences":[{"source":"PubMed","id":"38123684","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SO0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8TTB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	38
Details	Repeat: {"description":"HEAT 13","evidences":[{"source":"PubMed","id":"38123684","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SO0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8TTB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	38
Details	Repeat: {"description":"HEAT 14","evidences":[{"source":"PubMed","id":"38123684","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SO0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8TTB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P36873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"38123684","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SO0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8TTB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17055435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33243860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33633399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34762484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7K36","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7PKS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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