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4LAC

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

Functional Information from GO Data
ChainGOidnamespacecontents
B0019211molecular_functionphosphatase activator activity
C0000159cellular_componentprotein phosphatase type 2A complex
C0000278biological_processmitotic cell cycle
C0000775cellular_componentchromosome, centromeric region
C0000922cellular_componentspindle pole
C0001932biological_processregulation of protein phosphorylation
C0004721molecular_functionphosphoprotein phosphatase activity
C0004722molecular_functionprotein serine/threonine phosphatase activity
C0004725molecular_functionprotein tyrosine phosphatase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0006470biological_processprotein dephosphorylation
C0007498biological_processmesoderm development
C0008287cellular_componentprotein serine/threonine phosphatase complex
C0010288biological_processresponse to lead ion
C0010719biological_processnegative regulation of epithelial to mesenchymal transition
C0015630cellular_componentmicrotubule cytoskeleton
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0017018molecular_functionmyosin phosphatase activity
C0035331biological_processnegative regulation of hippo signaling
C0035556biological_processintracellular signal transduction
C0035970biological_processpeptidyl-threonine dephosphorylation
C0040008biological_processregulation of growth
C0043029biological_processT cell homeostasis
C0045121cellular_componentmembrane raft
C0045202cellular_componentsynapse
C0045595biological_processregulation of cell differentiation
C0046872molecular_functionmetal ion binding
C0046982molecular_functionprotein heterodimerization activity
C0048156molecular_functiontau protein binding
C0050811molecular_functionGABA receptor binding
C0051321biological_processmeiotic cell cycle
C0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
C0070062cellular_componentextracellular exosome
C0070262biological_processpeptidyl-serine dephosphorylation
C0071902biological_processpositive regulation of protein serine/threonine kinase activity
C0090443cellular_componentFAR/SIN/STRIPAK complex
C1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
C1904526biological_processregulation of microtubule binding
C1904528biological_processpositive regulation of microtubule binding
C1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
C2000045biological_processregulation of G1/S transition of mitotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 601
ChainResidue
AALA415
ALYS416
ATRP417
AARG420
AHOH716
AHOH719
CASP290

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 501
ChainResidue
CHIS167
CHIS241
CMN502
CAGS503
CASP85
CASN117

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 502
ChainResidue
CASP57
CHIS59
CASP85
CMN501
CAGS503

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE AGS C 503
ChainResidue
BARG148
BASP150
BGLY152
BTHR153
BGLY154
BPRO203
BALA204
BGLY205
BPRO304
BVAL305
BGLN307
BHIS308
CASP57
CHIS59
CASP85
CARG89
CASN117
CHIS118
CTYR127
CARG214
CHIS241
CMN501
CMN502
CHOH604
CHOH656

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES C 504
ChainResidue
CGLN61
CPHE62
CHIS63
CASP64
CPRO263
CASN264
CTYR267
CPRO291

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
CLEU114-GLU119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P36873
ChainResidueDetails
CHIS118
BTYR188
BLEU189

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17055435, ECO:0000269|PubMed:33633399, ECO:0007744|PDB:7K36
ChainResidueDetails
CASP57
CHIS59
CASP85
CASN117
CHIS167
CHIS241

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P67774
ChainResidueDetails
CTYR307

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Leucine methyl ester => ECO:0000269|PubMed:8206937
ChainResidueDetails
CLEU309

224572

PDB entries from 2024-09-04

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