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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6A5S

Structure of 14-3-3 gamma in complex with TFEB 14-3-3 binding motif

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
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
G0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
G0003723molecular_functionRNA binding
G0005080molecular_functionprotein kinase C binding
G0005159molecular_functioninsulin-like growth factor receptor binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005759cellular_componentmitochondrial matrix
G0005829cellular_componentcytosol
G0005925cellular_componentfocal adhesion
G0006469biological_processnegative regulation of protein kinase activity
G0007165biological_processsignal transduction
G0008104biological_processintracellular protein localization
G0008426molecular_functionprotein kinase C inhibitor activity
G0009966biological_processregulation of signal transduction
G0016020cellular_componentmembrane
G0019904molecular_functionprotein domain specific binding
G0022409biological_processpositive regulation of cell-cell adhesion
G0030971molecular_functionreceptor tyrosine kinase binding
G0031982cellular_componentvesicle
G0032869biological_processcellular response to insulin stimulus
G0032880biological_processregulation of protein localization
G0042149biological_processcellular response to glucose starvation
G0042802molecular_functionidentical protein binding
G0045202cellular_componentsynapse
G0045664biological_processregulation of neuron differentiation
G0048167biological_processregulation of synaptic plasticity
G0050870biological_processpositive regulation of T cell activation
G0070062cellular_componentextracellular exosome
G0098793cellular_componentpresynapse
G0140031molecular_functionphosphorylation-dependent protein binding
G0140311molecular_functionprotein sequestering activity
G1904262biological_processnegative regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue NA A 301
ChainResidue
ALYS120
AHOH409
GHOH370
site_idAC2
Number of Residues5
Detailsbinding site for residue MG B 301
ChainResidue
BASP202
BASP203
BALA204
BILE205
BALA206
site_idAC3
Number of Residues13
Detailsbinding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
ChainResidue
BARG57
BARG132
BTYR133
BGLY174
BLEU177
BASN178
BLEU225
CSER5
CPRO8
CHOH102
CHOH103
CHOH105
BLYS50
site_idAC4
Number of Residues16
Detailsbinding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
ChainResidue
ALYS50
AARG57
AARG132
ATYR133
AGLY174
ALEU177
AASN178
ALEU225
AHOH413
ESER5
EPRO8
EALA9
EHOH102
EHOH103
EHOH105
EHOH108
site_idAC5
Number of Residues13
Detailsbinding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
ChainResidue
DLYS50
DARG57
DARG132
DTYR133
DGLY174
DLEU177
DASN178
FSER5
FPRO8
FALA9
FHOH102
FHOH104
FHOH108
site_idAC6
Number of Residues13
Detailsbinding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
ChainResidue
GLYS50
GARG57
GARG132
GTYR133
GGLY174
GLEU177
GASN178
HSER5
HPRO8
HHOH101
HHOH103
HHOH106
HHOH107
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG42-VAL52
site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR216-SER235
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 Residues1
DetailsModified residue: {"description":"N-acetylvaline; partial","evidences":[{"source":"PubMed","id":"14534293","evidenceCode":"ECO:0000269"},{"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."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","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","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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