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1JK7

CRYSTAL STRUCTURE OF THE TUMOR-PROMOTER OKADAIC ACID BOUND TO PROTEIN PHOSPHATASE-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000070biological_processmitotic sister chromatid segregation
A0000165biological_processMAPK cascade
A0000775cellular_componentchromosome, centromeric region
A0000776cellular_componentkinetochore
A0000781cellular_componentchromosome, telomeric region
A0001824biological_processblastocyst development
A0003723molecular_functionRNA binding
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005515molecular_functionprotein binding
A0005521molecular_functionlamin binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005815cellular_componentmicrotubule organizing center
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005925cellular_componentfocal adhesion
A0005977biological_processglycogen metabolic process
A0006470biological_processprotein dephosphorylation
A0007283biological_processspermatogenesis
A0008157molecular_functionprotein phosphatase 1 binding
A0016607cellular_componentnuclear speck
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0017018molecular_functionmyosin phosphatase activity
A0019901molecular_functionprotein kinase binding
A0019903molecular_functionprotein phosphatase binding
A0019904molecular_functionprotein domain specific binding
A0030182biological_processneuron differentiation
A0030496cellular_componentmidbody
A0032154cellular_componentcleavage furrow
A0032922biological_processcircadian regulation of gene expression
A0032991cellular_componentprotein-containing complex
A0042752biological_processregulation of circadian rhythm
A0043153biological_processentrainment of circadian clock by photoperiod
A0043197cellular_componentdendritic spine
A0044877molecular_functionprotein-containing complex binding
A0046822biological_processregulation of nucleocytoplasmic transport
A0046872molecular_functionmetal ion binding
A0048511biological_processrhythmic process
A0051301biological_processcell division
A0060252biological_processpositive regulation of glial cell proliferation
A0072357cellular_componentPTW/PP1 phosphatase complex
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 400
ChainResidue
AASP92
AASN124
AHIS173
AHIS248
AMN401
AHOH2118

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AHIS248
AMN400
AHOH2118
AASP64
AHIS66
AASP92

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2022
ChainResidue
ALYS211
APHE258
AALA259
ALYS260
AHOH2053
AHOH2139

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE OKA A 501
ChainResidue
AARG96
AHIS125
AILE130
ATYR134
AGLN181
AARG188
AASP220
AARG221
ALYS234
AHIS237
ATYR272
ACYS273
AGLU275
APHE276
ABME2025
AHOH2119
AHOH2120
AHOH2131
AHOH2132
AHOH2133
AHOH2134

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 2023
ChainResidue
ATYR137
ALYS141
AARG261
AHOH2138

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 2024
ChainResidue
AILE169
ALEU289
AMET290
ACYS291

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 2025
ChainResidue
AASP208
AARG221
AGLN249
AOKA501
AHOH2123

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 Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:7500362
ChainResidueDetails
AHIS125

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11535607, ECO:0000269|PubMed:15280359
ChainResidueDetails
AASP64
AHIS66
AASP92
AASN124
AHIS173
AHIS248

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Inhibition by microcystin toxin binding
ChainResidueDetails
ACYS273

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR307

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR311

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
AASP95
AHIS125

222415

PDB entries from 2024-07-10

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