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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6ZBT

Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342

Functional Information from GO Data
ChainGOidnamespacecontents
A0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
A0003723molecular_functionRNA binding
A0005080molecular_functionprotein kinase C binding
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006469biological_processnegative regulation of protein kinase activity
A0007165biological_processsignal transduction
A0008104biological_processintracellular protein localization
A0008426molecular_functionprotein kinase C inhibitor activity
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0019904molecular_functionprotein domain specific binding
A0022409biological_processpositive regulation of cell-cell adhesion
A0030971molecular_functionreceptor tyrosine kinase binding
A0031982cellular_componentvesicle
A0032869biological_processcellular response to insulin stimulus
A0032880biological_processregulation of protein localization
A0042149biological_processcellular response to glucose starvation
A0042802molecular_functionidentical protein binding
A0045202cellular_componentsynapse
A0045664biological_processregulation of neuron differentiation
A0048167biological_processregulation of synaptic plasticity
A0050870biological_processpositive regulation of T cell activation
A0070062cellular_componentextracellular exosome
A0098793cellular_componentpresynapse
A0140031molecular_functionphosphorylation-dependent protein binding
A0140311molecular_functionprotein sequestering activity
A1904262biological_processnegative regulation of TORC1 signaling
B0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
B0003723molecular_functionRNA binding
B0005080molecular_functionprotein kinase C binding
B0005159molecular_functioninsulin-like growth factor receptor binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006469biological_processnegative regulation of protein kinase activity
B0007165biological_processsignal transduction
B0008104biological_processintracellular protein localization
B0008426molecular_functionprotein kinase C inhibitor activity
B0009966biological_processregulation of signal transduction
B0016020cellular_componentmembrane
B0019904molecular_functionprotein domain specific binding
B0022409biological_processpositive regulation of cell-cell adhesion
B0030971molecular_functionreceptor tyrosine kinase binding
B0031982cellular_componentvesicle
B0032869biological_processcellular response to insulin stimulus
B0032880biological_processregulation of protein localization
B0042149biological_processcellular response to glucose starvation
B0042802molecular_functionidentical protein binding
B0045202cellular_componentsynapse
B0045664biological_processregulation of neuron differentiation
B0048167biological_processregulation of synaptic plasticity
B0050870biological_processpositive regulation of T cell activation
B0070062cellular_componentextracellular exosome
B0098793cellular_componentpresynapse
B0140031molecular_functionphosphorylation-dependent protein binding
B0140311molecular_functionprotein sequestering activity
B1904262biological_processnegative regulation of TORC1 signaling
C0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
C0003723molecular_functionRNA binding
C0005080molecular_functionprotein kinase C binding
C0005159molecular_functioninsulin-like growth factor receptor binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005759cellular_componentmitochondrial matrix
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0006469biological_processnegative regulation of protein kinase activity
C0007165biological_processsignal transduction
C0008104biological_processintracellular protein localization
C0008426molecular_functionprotein kinase C inhibitor activity
C0009966biological_processregulation of signal transduction
C0016020cellular_componentmembrane
C0019904molecular_functionprotein domain specific binding
C0022409biological_processpositive regulation of cell-cell adhesion
C0030971molecular_functionreceptor tyrosine kinase binding
C0031982cellular_componentvesicle
C0032869biological_processcellular response to insulin stimulus
C0032880biological_processregulation of protein localization
C0042149biological_processcellular response to glucose starvation
C0042802molecular_functionidentical protein binding
C0045202cellular_componentsynapse
C0045664biological_processregulation of neuron differentiation
C0048167biological_processregulation of synaptic plasticity
C0050870biological_processpositive regulation of T cell activation
C0070062cellular_componentextracellular exosome
C0098793cellular_componentpresynapse
C0140031molecular_functionphosphorylation-dependent protein binding
C0140311molecular_functionprotein sequestering activity
C1904262biological_processnegative regulation of TORC1 signaling
D0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
D0003723molecular_functionRNA binding
D0005080molecular_functionprotein kinase C binding
D0005159molecular_functioninsulin-like growth factor receptor binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005759cellular_componentmitochondrial matrix
D0005829cellular_componentcytosol
D0005925cellular_componentfocal adhesion
D0006469biological_processnegative regulation of protein kinase activity
D0007165biological_processsignal transduction
D0008104biological_processintracellular protein localization
D0008426molecular_functionprotein kinase C inhibitor activity
D0009966biological_processregulation of signal transduction
D0016020cellular_componentmembrane
D0019904molecular_functionprotein domain specific binding
D0022409biological_processpositive regulation of cell-cell adhesion
D0030971molecular_functionreceptor tyrosine kinase binding
D0031982cellular_componentvesicle
D0032869biological_processcellular response to insulin stimulus
D0032880biological_processregulation of protein localization
D0042149biological_processcellular response to glucose starvation
D0042802molecular_functionidentical protein binding
D0045202cellular_componentsynapse
D0045664biological_processregulation of neuron differentiation
D0048167biological_processregulation of synaptic plasticity
D0050870biological_processpositive regulation of T cell activation
D0070062cellular_componentextracellular exosome
D0098793cellular_componentpresynapse
D0140031molecular_functionphosphorylation-dependent protein binding
D0140311molecular_functionprotein sequestering activity
D1904262biological_processnegative regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CFH A 301
ChainResidue
APHE201
AASP202
ACFH302
CPHE201
CARG227
site_idAC2
Number of Residues6
Detailsbinding site for residue CFH A 302
ChainResidue
CPHE201
CASP202
APHE201
AARG227
ACFH301
CLYS198
site_idAC3
Number of Residues7
Detailsbinding site for residue CFH B 301
ChainResidue
BLEU208
BASP209
CILE66
CLYS78
DGLN9
DARG12
DLEU13
site_idAC4
Number of Residues10
Detailsbinding site for residue CFH D 301
ChainResidue
AILE66
ATHR70
ALYS78
AMET81
BGLN9
BARG12
BLEU13
DILE205
DLEU208
DASP209
site_idAC5
Number of Residues15
Detailsbinding site for Di-peptide CYS E 341 and SEP E 342
ChainResidue
ALYS50
AARG57
AARG132
ATYR133
ALEU177
AASN178
AVAL181
AASN229
EARG339
ESER340
EVAL343
ETHR344
EHOH401
EHOH402
EHOH403
site_idAC6
Number of Residues12
Detailsbinding site for Di-peptide SEP E 342 and VAL E 343
ChainResidue
ALYS50
AARG57
AARG132
ATYR133
AGLY174
ALEU177
AASN178
ECYS341
ETHR344
EHOH401
EHOH402
EHOH403
site_idAC7
Number of Residues15
Detailsbinding site for Di-peptide CYS F 341 and SEP F 342
ChainResidue
CLYS50
CARG57
CARG132
CTYR133
CLEU177
CASN178
CVAL181
CASN229
FARG339
FSER340
FVAL343
FTHR344
FHOH402
FHOH403
FHOH404
site_idAC8
Number of Residues12
Detailsbinding site for Di-peptide SEP F 342 and VAL F 343
ChainResidue
CLYS50
CARG57
CARG132
CTYR133
CGLY174
CLEU177
CASN178
FCYS341
FTHR344
FHOH402
FHOH403
FHOH404
site_idAC9
Number of Residues14
Detailsbinding site for Di-peptide CYS G 341 and SEP G 342
ChainResidue
BLYS50
BARG57
BARG132
BTYR133
BLEU177
BASN178
BVAL181
BASN229
GSER340
GVAL343
GTHR344
GHOH401
GHOH402
GHOH403
site_idAD1
Number of Residues12
Detailsbinding site for Di-peptide SEP G 342 and VAL G 343
ChainResidue
BTYR133
BGLY174
BLEU177
BASN178
GCYS341
GTHR344
GHOH401
GHOH402
GHOH403
BLYS50
BARG57
BARG132
site_idAD2
Number of Residues13
Detailsbinding site for Di-peptide CYS H 341 and SEP H 342
ChainResidue
DLYS50
DARG57
DARG132
DTYR133
DLEU177
DASN178
DVAL181
DASN229
HSER340
HVAL343
HTHR344
HHOH401
HHOH402
site_idAD3
Number of Residues12
Detailsbinding site for Di-peptide SEP H 342 and VAL H 343
ChainResidue
DLYS50
DARG57
DARG132
DTYR133
DGLY174
DLEU177
DASN178
HSER340
HCYS341
HTHR344
HHOH401
HHOH402
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG42-VAL52
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"PubMed","id":"17085597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by WNK1 and WNK4","evidences":[{"source":"PubMed","id":"15328345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20525693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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