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1IT6

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000070biological_processmitotic sister chromatid segregation
A0000164cellular_componentprotein phosphatase type 1 complex
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
B0000070biological_processmitotic sister chromatid segregation
B0000164cellular_componentprotein phosphatase type 1 complex
B0000165biological_processMAPK cascade
B0000776cellular_componentkinetochore
B0000781cellular_componentchromosome, telomeric region
B0003723molecular_functionRNA binding
B0004721molecular_functionphosphoprotein phosphatase activity
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0005515molecular_functionprotein binding
B0005521molecular_functionlamin binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005815cellular_componentmicrotubule organizing center
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0005977biological_processglycogen metabolic process
B0006470biological_processprotein dephosphorylation
B0008157molecular_functionprotein phosphatase 1 binding
B0016607cellular_componentnuclear speck
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0019901molecular_functionprotein kinase binding
B0019903molecular_functionprotein phosphatase binding
B0019904molecular_functionprotein domain specific binding
B0030182biological_processneuron differentiation
B0030496cellular_componentmidbody
B0032154cellular_componentcleavage furrow
B0032922biological_processcircadian regulation of gene expression
B0032991cellular_componentprotein-containing complex
B0042752biological_processregulation of circadian rhythm
B0043153biological_processentrainment of circadian clock by photoperiod
B0043197cellular_componentdendritic spine
B0044877molecular_functionprotein-containing complex binding
B0046579biological_processpositive regulation of Ras protein signal transduction
B0046872molecular_functionmetal ion binding
B0048511biological_processrhythmic process
B0051301biological_processcell division
B0060252biological_processpositive regulation of glial cell proliferation
B0072357cellular_componentPTW/PP1 phosphatase complex
B0098793cellular_componentpresynapse
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AASP64
AHIS66
AASP92
AMN402
AHOH601
AHOH602

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AHIS248
AMN401
AHOH601
AASP92
AASN124
AHIS173

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BASP64
BHIS66
BASP92
BMN402
BHOH603
BHOH604

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
BASP92
BASN124
BHIS173
BHIS248
BMN401
BHOH603

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE CYU A 501
ChainResidue
AARG96
ASER129
AILE130
ATYR134
AVAL195
APRO196
AASP197
AASP208
APRO209
AASN219
AASP220
AARG221
AVAL223
ATHR226
AHIS248
AGLN249
ATYR272
AHOH601
AHOH602
AHOH607
AHOH608
AHOH612
BARG132
BLYS141
BHOH670

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE CYU B 1501
ChainResidue
AARG132
ALYS141
AHOH676
BARG96
BSER129
BILE130
BTYR134
BVAL195
BPRO196
BASP197
BASN219
BASP220
BARG221
BTHR226
BHIS248
BGLN249
BTYR272
BHOH603
BHOH604
BHOH614
BHOH615
BHOH642

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":"PubMed","id":"7500362","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
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 Residues2
DetailsSite: {"description":"Inhibition by microcystin toxin binding"}
ChainResidueDetails

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
BASP95
BHIS125

246031

PDB entries from 2025-12-10

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