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5INB

RepoMan-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000070biological_processmitotic sister chromatid segregation
A0000165biological_processMAPK cascade
A0000776cellular_componentkinetochore
A0000781cellular_componentchromosome, telomeric region
A0003723molecular_functionRNA binding
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005515molecular_functionprotein binding
A0005521molecular_functionlamin binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005815cellular_componentmicrotubule organizing center
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0005977biological_processglycogen metabolic process
A0006470biological_processprotein dephosphorylation
A0008157molecular_functionprotein phosphatase 1 binding
A0016607cellular_componentnuclear speck
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase 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
A0046579biological_processpositive regulation of Ras protein signal transduction
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 Residues12
Detailsbinding site for residue MLI A 401
ChainResidue
AASP64
AHOH538
AHOH542
AHOH614
AHIS66
AASP92
AGLU218
AASP220
AARG221
AHIS248
ATYR272
AGOL402

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 402
ChainResidue
AGLU218
AASN219
AASP220
AGLN249
AVAL250
AMLI401
AHOH513
AHOH598
AHOH630

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 403
ChainResidue
AGLN185
AARG188
ASER224
APHE225
AHOH505
AHOH516
AHOH520

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 404
ChainResidue
ACYS127
ASER129
AVAL195
APRO196
AASP197
ACYS202
ATRP206
AHOH649

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL A 405
ChainResidue
APRO50
ALEU53
AGLU54
AGLU116
APHE119
ALYS141
AHOH621
AHOH653
AHOH674

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL A 406
ChainResidue
APRO58
ALEU59
ALYS60
ASER85
AASN86
ASER284
AVAL285
AHOH528

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL A 407
ChainResidue
APRO209
AGLN249
AVAL251
AGLU256
AHOH515
AHOH552
AHOH577
AHOH592

site_idAC8
Number of Residues4
Detailsbinding site for residue NA A 408
ChainResidue
AGLU54
AILE164
AGLU167
AHOH721

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
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"7500362","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11535607","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15280359","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35768504","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7SD0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Inhibition by microcystin toxin binding"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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