Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4GNT

Complex of ChREBP and 14-3-3beta

Functional Information from GO Data
ChainGOidnamespacecontents
A0004860molecular_functionprotein kinase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006605biological_processprotein targeting
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
A0045184biological_processestablishment of protein localization
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
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ALYS51
AARG58
AARG129
ATYR130
AHOH432
AHOH433
BTRP127
BARG128

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AGLU37
AHIS36

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AGLN113
AALA114

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
ASER39
AASN40
AHOH416
AHOH454

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interaction with phosphoserine on interacting protein => ECO:0000250
ChainResidueDetails
AARG58
AARG129

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
AMET1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
ATHR2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS5

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS51

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9705322
ChainResidueDetails
ASER60

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
ALYS70
ALYS117

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0007744|PubMed:16800626
ChainResidueDetails
ATYR84
ATYR106

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68251
ChainResidueDetails
ASER186

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
ASER232

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS51

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon