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6OBN

The crystal structure of coexpressed SDS22:PP1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000164cellular_componentprotein phosphatase type 1 complex
A0000781cellular_componentchromosome, telomeric region
A0001111biological_processRNA polymerase II promoter clearance
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
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005912cellular_componentadherens junction
A0005977biological_processglycogen metabolic process
A0005979biological_processregulation of glycogen biosynthetic process
A0005981biological_processregulation of glycogen catabolic process
A0006470biological_processprotein dephosphorylation
A0008157molecular_functionprotein phosphatase 1 binding
A0010288biological_processresponse to lead ion
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0032922biological_processcircadian regulation of gene expression
A0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
A0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
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
A0043558biological_processregulation of translational initiation in response to stress
A0044877molecular_functionprotein-containing complex binding
A0045725biological_processpositive regulation of glycogen biosynthetic process
A0046579biological_processpositive regulation of Ras protein signal transduction
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0050821biological_processprotein stabilization
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
A0180007molecular_functionRNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
A2000806biological_processpositive regulation of termination of RNA polymerase II transcription, poly(A)-coupled
B0000164cellular_componentprotein phosphatase type 1 complex
B0000781cellular_componentchromosome, telomeric region
B0001111biological_processRNA polymerase II promoter clearance
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
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0005912cellular_componentadherens junction
B0005977biological_processglycogen metabolic process
B0005979biological_processregulation of glycogen biosynthetic process
B0005981biological_processregulation of glycogen catabolic process
B0006470biological_processprotein dephosphorylation
B0008157molecular_functionprotein phosphatase 1 binding
B0010288biological_processresponse to lead ion
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0032922biological_processcircadian regulation of gene expression
B0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
B0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
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
B0043558biological_processregulation of translational initiation in response to stress
B0044877molecular_functionprotein-containing complex binding
B0045725biological_processpositive regulation of glycogen biosynthetic process
B0046579biological_processpositive regulation of Ras protein signal transduction
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0050821biological_processprotein stabilization
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
B0180007molecular_functionRNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
B2000806biological_processpositive regulation of termination of RNA polymerase II transcription, poly(A)-coupled
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PO4 A 401
ChainResidue
AHIS66
AASP92
AASN124
AHIS125
AARG221
AHIS248
ATYR272
AFE403
AHOH505

site_idAC2
Number of Residues3
Detailsbinding site for residue PO4 A 402
ChainResidue
AILE295
ALYS297
BCYS291

site_idAC3
Number of Residues6
Detailsbinding site for residue FE A 403
ChainResidue
AASP92
AASN124
AHIS173
AHIS248
APO4401
AHOH505

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
AMET183
AHIS239

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 405
ChainResidue
AARG191
AHOH506
DLYS342

site_idAC6
Number of Residues1
Detailsbinding site for residue MPD A 406
ChainResidue
ACYS291

site_idAC7
Number of Residues3
Detailsbinding site for residue MPD A 407
ChainResidue
ASER4
AASN8
AASN33

site_idAC8
Number of Residues8
Detailsbinding site for residue PO4 B 401
ChainResidue
BHIS66
BASP92
BASN124
BHIS125
BARG221
BHIS248
BFE402
BHOH501

site_idAC9
Number of Residues6
Detailsbinding site for residue FE B 402
ChainResidue
BASP92
BASN124
BHIS173
BHIS248
BPO4401
BHOH501

site_idAD1
Number of Residues2
Detailsbinding site for residue CL B 403
ChainResidue
BARG191
CLYS342

site_idAD2
Number of Residues3
Detailsbinding site for residue PO4 C 401
ChainResidue
CARG199
CLYS219
CARG241

site_idAD3
Number of Residues3
Detailsbinding site for residue PO4 C 402
ChainResidue
CARG155
CLYS175
CARG197

site_idAD4
Number of Residues2
Detailsbinding site for residue PO4 C 403
ChainResidue
CGLU309
CPRO332

site_idAD5
Number of Residues2
Detailsbinding site for residue MPD C 404
ChainResidue
CGLN334
DLYS335

site_idAD6
Number of Residues4
Detailsbinding site for residue MPD C 405
ChainResidue
ALYS6
AASP10
CGLU324
CARG351

site_idAD7
Number of Residues4
Detailsbinding site for residue PO4 D 401
ChainResidue
AASP212
DARG199
DLYS219
DARG241

site_idAD8
Number of Residues3
Detailsbinding site for residue PO4 D 402
ChainResidue
DARG155
DLYS175
DARG197

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
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P36873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30100357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35830882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35831509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36175670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39446389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8SW5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues42
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues42
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues42
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues42
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues42
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues42
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues42
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues42
DetailsRepeat: {"description":"LRR 8"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues42
DetailsRepeat: {"description":"LRR 9"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues42
DetailsRepeat: {"description":"LRR 10"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues42
DetailsRepeat: {"description":"LRR 11"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues29
DetailsDomain: {"description":"LRRCT"}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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