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6YGJ

small-molecule stabilizer of 14-3-3 and the Carbohydrate Response Element Binding Protein (ChREBP) protein-protein interaction

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
F0004860molecular_functionprotein kinase inhibitor activity
F0004864molecular_functionprotein phosphatase inhibitor activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005774cellular_componentvacuolar membrane
F0005829cellular_componentcytosol
F0005925cellular_componentfocal adhesion
F0007165biological_processsignal transduction
F0008104biological_processintracellular protein localization
F0016020cellular_componentmembrane
F0017053cellular_componenttranscription repressor complex
F0019899molecular_functionenzyme binding
F0019904molecular_functionprotein domain specific binding
F0032991cellular_componentprotein-containing complex
F0042308biological_processnegative regulation of protein import into nucleus
F0042470cellular_componentmelanosome
F0042802molecular_functionidentical protein binding
F0042826molecular_functionhistone deacetylase binding
F0044877molecular_functionprotein-containing complex binding
F0045296molecular_functioncadherin binding
F0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
F0045892biological_processnegative regulation of DNA-templated transcription
F0045944biological_processpositive regulation of transcription by RNA polymerase II
F0048471cellular_componentperinuclear region of cytoplasm
F0050815molecular_functionphosphoserine residue binding
F0051219molecular_functionphosphoprotein binding
F0070062cellular_componentextracellular exosome
F0140311molecular_functionprotein sequestering activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue OQE A 301
ChainResidue
ALYS51
AARG58
AARG129
ATYR130
BILE120
BASN124
BTRP127
BARG128

site_idAC2
Number of Residues8
Detailsbinding site for residue OQE F 301
ChainResidue
FARG58
FARG129
FTYR130
FLEU174
IASN124
ITRP127
IARG128
FLYS51

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
FARG43-VAL53
AARG43-VAL53

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
FTYR213-SER232
ATYR213-SER232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68251","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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