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5WFU

Structural basis for the interaction of 14-3-3beta with Tricarboxylic Acid Cycle intermediate Malate

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
B0004860molecular_functionprotein kinase inhibitor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006605biological_processprotein targeting
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
B0045184biological_processestablishment of protein localization
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
C0004860molecular_functionprotein kinase inhibitor activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006605biological_processprotein targeting
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
C0045184biological_processestablishment of protein localization
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
D0004860molecular_functionprotein kinase inhibitor activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006605biological_processprotein targeting
D0019899molecular_functionenzyme binding
D0019904molecular_functionprotein domain specific binding
D0035308biological_processnegative regulation of protein dephosphorylation
D0042470cellular_componentmelanosome
D0042802molecular_functionidentical protein binding
D0042826molecular_functionhistone deacetylase binding
D0043085biological_processpositive regulation of catalytic activity
D0045184biological_processestablishment of protein localization
D0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
D0048471cellular_componentperinuclear region of cytoplasm
D0050815molecular_functionphosphoserine residue binding
D0051219molecular_functionphosphoprotein binding
D0051220biological_processcytoplasmic sequestering of protein
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue MLT A 301
ChainResidue
ATHR32
ATYR120
AHOH402
AHOH415
AGLY35
AHIS36
AGLU37
ALEU38
ATYR106
ALEU107
AASN110
AALA111

site_idAC2
Number of Residues10
Detailsbinding site for residue MLT B 301
ChainResidue
BTHR32
BGLY35
BHIS36
BGLU37
BLEU38
BTYR106
BLEU107
BASN110
BALA111
BTYR120

site_idAC3
Number of Residues12
Detailsbinding site for residue MLT C 301
ChainResidue
CTHR32
CGLY35
CHIS36
CGLU37
CLEU38
CTYR106
CLEU107
CASN110
CALA111
CTYR120
CHOH403
CHOH417

site_idAC4
Number of Residues10
Detailsbinding site for residue MLT D 301
ChainResidue
DTHR32
DGLY35
DHIS36
DGLU37
DLEU38
DTYR106
DLEU107
DASN110
DALA111
DTYR120

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 Residues8
DetailsSITE: Interaction with phosphoserine on interacting protein => ECO:0000250
ChainResidueDetails
AARG58
AARG129
BARG58
BARG129
CARG58
CARG129
DARG58
DARG129

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
AMET1
BMET1
CMET1
DMET1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
ATHR2
BTHR2
CTHR2
DTHR2

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS5
BLYS5
CLYS5
DLYS5

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS51
BLYS51
CLYS51
DLYS51

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9705322
ChainResidueDetails
ASER60
BSER60
CSER60
DSER60

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
ALYS70
ALYS117
BLYS70
BLYS117
CLYS70
CLYS117
DLYS70
DLYS117

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0007744|PubMed:16800626
ChainResidueDetails
ATYR84
ATYR106
BTYR84
BTYR106
CTYR84
CTYR106
DTYR84
DTYR106

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68251
ChainResidueDetails
ASER186
BSER186
CSER186
DSER186

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P31946
ChainResidueDetails
ASER232
BSER232
CSER232
DSER232

site_idSWS_FT_FI11
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS51
BLYS51
CLYS51
DLYS51

224931

PDB entries from 2024-09-11

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