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6GHM

Structure of PP1 alpha phosphatase bound to ASPP2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000164cellular_componentprotein phosphatase type 1 complex
A0000781cellular_componentchromosome, telomeric region
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0005977biological_processglycogen metabolic process
A0005979biological_processregulation of glycogen biosynthetic process
A0005981biological_processregulation of glycogen catabolic process
A0006446biological_processregulation of translational initiation
A0006470biological_processprotein dephosphorylation
A0008157molecular_functionprotein phosphatase 1 binding
A0010288biological_processresponse to lead ion
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0017018molecular_functionmyosin phosphatase activity
A0030324biological_processlung development
A0032922biological_processcircadian regulation of gene expression
A0042587cellular_componentglycogen granule
A0042752biological_processregulation of circadian rhythm
A0043021molecular_functionribonucleoprotein complex binding
A0043025cellular_componentneuronal cell body
A0043153biological_processentrainment of circadian clock by photoperiod
A0043197cellular_componentdendritic spine
A0043204cellular_componentperikaryon
A0043247biological_processtelomere maintenance in response to DNA damage
A0044877molecular_functionprotein-containing complex binding
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0048754biological_processbranching morphogenesis of an epithelial tube
A0051301biological_processcell division
A0060828biological_processregulation of canonical Wnt signaling pathway
A0070062cellular_componentextracellular exosome
A0072357cellular_componentPTW/PP1 phosphatase complex
A0098609biological_processcell-cell adhesion
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A2001241biological_processpositive regulation of extrinsic apoptotic signaling pathway in absence of ligand
B0000164cellular_componentprotein phosphatase type 1 complex
B0000781cellular_componentchromosome, telomeric region
B0004721molecular_functionphosphoprotein phosphatase activity
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005912cellular_componentadherens junction
B0005977biological_processglycogen metabolic process
B0005979biological_processregulation of glycogen biosynthetic process
B0005981biological_processregulation of glycogen catabolic process
B0006446biological_processregulation of translational initiation
B0006470biological_processprotein dephosphorylation
B0008157molecular_functionprotein phosphatase 1 binding
B0010288biological_processresponse to lead ion
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0017018molecular_functionmyosin phosphatase activity
B0030324biological_processlung development
B0032922biological_processcircadian regulation of gene expression
B0042587cellular_componentglycogen granule
B0042752biological_processregulation of circadian rhythm
B0043021molecular_functionribonucleoprotein complex binding
B0043025cellular_componentneuronal cell body
B0043153biological_processentrainment of circadian clock by photoperiod
B0043197cellular_componentdendritic spine
B0043204cellular_componentperikaryon
B0043247biological_processtelomere maintenance in response to DNA damage
B0044877molecular_functionprotein-containing complex binding
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0048754biological_processbranching morphogenesis of an epithelial tube
B0051301biological_processcell division
B0060828biological_processregulation of canonical Wnt signaling pathway
B0070062cellular_componentextracellular exosome
B0072357cellular_componentPTW/PP1 phosphatase complex
B0098609biological_processcell-cell adhesion
B0098641molecular_functioncadherin binding involved in cell-cell adhesion
B0098793cellular_componentpresynapse
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B2001241biological_processpositive regulation of extrinsic apoptotic signaling pathway in absence of ligand
C0002039molecular_functionp53 binding
C0042981biological_processregulation of apoptotic process
D0002039molecular_functionp53 binding
D0042981biological_processregulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 401
ChainResidue
AASP208
AGLU218
AASN219
AASP220
ATHR226
AGLN249

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 402
ChainResidue
AASP10
BPRO82
BGLU84
BHOH502
ALEU7
AASN8
ALEU9

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 403
ChainResidue
ASER177
ALEU180
APHE235
AHOH527

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO A 404
ChainResidue
AGLU54
AGLU116

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
AGLN249
AGLU256
AHOH526

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 406
ChainResidue
AGLY67
AGLN68
ATYR69
ATYR70
AGLY97
ALYS98
AGLN99

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 407
ChainResidue
AASP253
ATYR255
AGLU256
APHE257
DASP932
DHOH1301

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL A 408
ChainResidue
AGLU56
AALA57
AASP166
AGLU287

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL A 409
ChainResidue
AILE130
ATYR134
AARG221
BPRO178
BASP179

site_idAD1
Number of Residues8
Detailsbinding site for residue NHE A 410
ChainResidue
ASER129
AILE130
AVAL195
APRO196
AASP197
ATRP206
AHOH506
BGLN181

site_idAD2
Number of Residues13
Detailsbinding site for residue NHE A 411
ChainResidue
AHIS66
AASP92
AARG96
AASN124
AHIS125
AARG221
AHIS248
AGLN249
AVAL250
AMN412
AMN413
AHOH501
AHOH551

site_idAD3
Number of Residues7
Detailsbinding site for residue MN A 412
ChainResidue
AASP64
AHIS66
AASP92
ANHE411
AMN413
AHOH501
AHOH551

site_idAD4
Number of Residues7
Detailsbinding site for residue MN A 413
ChainResidue
AASP92
AASN124
AHIS173
AHIS248
ANHE411
AMN412
AHOH501

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO B 401
ChainResidue
BLYS41
BGLU44
BILE45
BSER48

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO B 402
ChainResidue
BLEU47
BMET190
BARG191
BHOH519

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO B 403
ChainResidue
BGLN249
BGLU256
BPHE257
BHOH528

site_idAD8
Number of Residues5
Detailsbinding site for residue EDO B 404
ChainResidue
BASP253
BTYR255
BGLU256
BPHE257
CHOH1201

site_idAD9
Number of Residues3
Detailsbinding site for residue GOL B 405
ChainResidue
AGLY215
ATRP216
BSER129

site_idAE1
Number of Residues14
Detailsbinding site for residue NHE B 406
ChainResidue
BHIS66
BASP92
BARG96
BASN124
BHIS125
BARG221
BHIS248
BGLN249
BVAL250
BTYR272
BMN409
BMN410
BHOH511
BHOH538

site_idAE2
Number of Residues7
Detailsbinding site for residue NHE B 407
ChainResidue
ALYS234
BSER129
BVAL195
BPRO196
BASP197
BTRP206
BHOH540

site_idAE3
Number of Residues5
Detailsbinding site for residue NHE B 408
ChainResidue
BASP242
BLYS260
BARG261
CVAL922
CPHE924

site_idAE4
Number of Residues7
Detailsbinding site for residue MN B 409
ChainResidue
BASP64
BHIS66
BASP92
BNHE406
BMN410
BHOH511
BHOH538

site_idAE5
Number of Residues7
Detailsbinding site for residue MN B 410
ChainResidue
BASP92
BASN124
BHIS173
BHIS248
BNHE406
BMN409
BHOH511

site_idAE6
Number of Residues5
Detailsbinding site for residue EDO D 1201
ChainResidue
DASN1058
DVAL1061
DTYR1063
DLEU1116
DTYR1117

site_idAE7
Number of Residues4
Detailsbinding site for residue EDO D 1202
ChainResidue
DCYS1002
DASN1003
DASN1004
DGLU1038

site_idAE8
Number of Residues6
Detailsbinding site for residue NHE D 1203
ChainResidue
ALYS150
DGLY1055
DILE1056
DILE1086
DILE1087
DHIS1088

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU121-GLU126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS125
BHIS125

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP64
AHIS66
BASP64
BHIS66

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASP92
AASN124
AHIS173
AHIS248
BASP92
BASN124
BHIS173
BHIS248

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER22
ASER325
BSER22
BSER325

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62137
ChainResidueDetails
ALYS305
BLYS305

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62137
ChainResidueDetails
ATYR306
BTYR306

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:16732323, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR320
BTHR320

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PDB entries from 2024-07-24

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