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6A5Q

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004860molecular_functionprotein kinase inhibitor activity
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005774cellular_componentvacuolar membrane
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0007165biological_processsignal transduction
A0008104biological_processintracellular protein localization
A0016020cellular_componentmembrane
A0017053cellular_componenttranscription repressor complex
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0032991cellular_componentprotein-containing complex
A0042308biological_processnegative regulation of protein import into nucleus
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042826molecular_functionhistone deacetylase binding
A0044877molecular_functionprotein-containing complex binding
A0045296molecular_functioncadherin binding
A0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
A0045892biological_processnegative regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0048471cellular_componentperinuclear region of cytoplasm
A0050815molecular_functionphosphoserine residue binding
A0051219molecular_functionphosphoprotein binding
A0070062cellular_componentextracellular exosome
A0140311molecular_functionprotein sequestering activity
B0004860molecular_functionprotein kinase inhibitor activity
B0004864molecular_functionprotein phosphatase inhibitor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005774cellular_componentvacuolar membrane
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0007165biological_processsignal transduction
B0008104biological_processintracellular protein localization
B0016020cellular_componentmembrane
B0017053cellular_componenttranscription repressor complex
B0019899molecular_functionenzyme binding
B0019904molecular_functionprotein domain specific binding
B0032991cellular_componentprotein-containing complex
B0042308biological_processnegative regulation of protein import into nucleus
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0042826molecular_functionhistone deacetylase binding
B0044877molecular_functionprotein-containing complex binding
B0045296molecular_functioncadherin binding
B0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
B0045892biological_processnegative regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0048471cellular_componentperinuclear region of cytoplasm
B0050815molecular_functionphosphoserine residue binding
B0051219molecular_functionphosphoprotein binding
B0070062cellular_componentextracellular exosome
B0140311molecular_functionprotein sequestering activity
C0004860molecular_functionprotein kinase inhibitor activity
C0004864molecular_functionprotein phosphatase inhibitor activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005774cellular_componentvacuolar membrane
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0007165biological_processsignal transduction
C0008104biological_processintracellular protein localization
C0016020cellular_componentmembrane
C0017053cellular_componenttranscription repressor complex
C0019899molecular_functionenzyme binding
C0019904molecular_functionprotein domain specific binding
C0032991cellular_componentprotein-containing complex
C0042308biological_processnegative regulation of protein import into nucleus
C0042470cellular_componentmelanosome
C0042802molecular_functionidentical protein binding
C0042826molecular_functionhistone deacetylase binding
C0044877molecular_functionprotein-containing complex binding
C0045296molecular_functioncadherin binding
C0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
C0045892biological_processnegative regulation of DNA-templated transcription
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0048471cellular_componentperinuclear region of cytoplasm
C0050815molecular_functionphosphoserine residue binding
C0051219molecular_functionphosphoprotein binding
C0070062cellular_componentextracellular exosome
C0140311molecular_functionprotein sequestering activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MLA B 301
ChainResidue
BPHE198
BTHR217
BMET220
BGLN221
BARG224
BHOH421
CTYR213

site_idAC2
Number of Residues7
Detailsbinding site for residue MLA A 301
ChainResidue
AMET220
AGLN221
AARG224
AHOH415
BTYR213
APHE198
ATHR217

site_idAC3
Number of Residues7
Detailsbinding site for residue MLA C 301
ChainResidue
ATYR213
CPHE198
CTHR217
CMET220
CGLN221
CARG224
CHOH410

site_idAC4
Number of Residues16
Detailsbinding site for Ligand residues SEP D 6 through CYS D 7 bound to SER D 5
ChainResidue
CLYS51
CARG58
CARG129
CTYR130
CGLY171
CLEU174
CASN175
DSER5
DPRO8
DALA9
DLEU11
DHOH102
DHOH103
DHOH104
DHOH105
DHOH106

site_idAC5
Number of Residues16
Detailsbinding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
ChainResidue
BLYS51
BARG58
BARG129
BTYR130
BGLY171
BLEU174
BASN175
BLEU222
BHOH477
ESER5
EPRO8
EALA9
EHOH102
EHOH104
EHOH105
EHOH108

site_idAC6
Number of Residues17
Detailsbinding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
ChainResidue
ALYS51
AARG58
AARG129
ATYR130
AGLY171
ALEU174
AASN175
ALEU222
AHOH418
FSER5
FPRO8
FALA9
FLEU11
FHOH101
FHOH103
FHOH104
FHOH105

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
BARG43-VAL53

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
BTYR213-SER232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68251","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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