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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
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005773cellular_componentvacuole
A0005774cellular_componentvacuolar membrane
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006605biological_processprotein targeting
A0007165biological_processsignal transduction
A0008104biological_processprotein localization
A0016020cellular_componentmembrane
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0035308biological_processnegative regulation of protein dephosphorylation
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042826molecular_functionhistone deacetylase binding
A0043085biological_processpositive regulation of catalytic activity
A0045296molecular_functioncadherin binding
A0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
A0048471cellular_componentperinuclear region of cytoplasm
A0050815molecular_functionphosphoserine residue binding
A0051219molecular_functionphosphoprotein binding
A0051220biological_processcytoplasmic sequestering of protein
A0070062cellular_componentextracellular exosome
B0004860molecular_functionprotein kinase inhibitor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005773cellular_componentvacuole
B0005774cellular_componentvacuolar membrane
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006605biological_processprotein targeting
B0007165biological_processsignal transduction
B0008104biological_processprotein localization
B0016020cellular_componentmembrane
B0019899molecular_functionenzyme binding
B0019904molecular_functionprotein domain specific binding
B0035308biological_processnegative regulation of protein dephosphorylation
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0042826molecular_functionhistone deacetylase binding
B0043085biological_processpositive regulation of catalytic activity
B0045296molecular_functioncadherin binding
B0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
B0048471cellular_componentperinuclear region of cytoplasm
B0050815molecular_functionphosphoserine residue binding
B0051219molecular_functionphosphoprotein binding
B0051220biological_processcytoplasmic sequestering of protein
B0070062cellular_componentextracellular exosome
C0004860molecular_functionprotein kinase inhibitor activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005773cellular_componentvacuole
C0005774cellular_componentvacuolar membrane
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0006605biological_processprotein targeting
C0007165biological_processsignal transduction
C0008104biological_processprotein localization
C0016020cellular_componentmembrane
C0019899molecular_functionenzyme binding
C0019904molecular_functionprotein domain specific binding
C0035308biological_processnegative regulation of protein dephosphorylation
C0042470cellular_componentmelanosome
C0042802molecular_functionidentical protein binding
C0042826molecular_functionhistone deacetylase binding
C0043085biological_processpositive regulation of catalytic activity
C0045296molecular_functioncadherin binding
C0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
C0048471cellular_componentperinuclear region of cytoplasm
C0050815molecular_functionphosphoserine residue binding
C0051219molecular_functionphosphoprotein binding
C0051220biological_processcytoplasmic sequestering of protein
C0070062cellular_componentextracellular exosome
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: Interaction with phosphoserine on interacting protein => ECO:0000250
ChainResidueDetails
BARG58
BARG129
AARG58
AARG129
CARG58
CARG129

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate => ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378
ChainResidueDetails
BMET1
AMET1
CMET1

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR2
ATHR2
CTHR2

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
BLYS5
ALYS5
CLYS5

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
BLYS51
ALYS51
CLYS51

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CQV8
ChainResidueDetails
BSER60
ASER60
CSER60

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS70
BLYS117
ALYS70
ALYS117
CLYS70
CLYS117

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q9CQV8
ChainResidueDetails
BTYR84
BTYR106
ATYR84
ATYR106
CTYR84
CTYR106

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68251
ChainResidueDetails
BSER186
ASER186
CSER186

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER232
ASER232
CSER232

site_idSWS_FT_FI11
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
BLYS51
ALYS51
CLYS51

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PDB entries from 2024-07-31

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