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6GNK

Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, trimeric crystal form bound to Carba-NAD

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
C0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue CNA C 501
ChainResidue
AGLU233
CARG322
CGLY323
CGLY324
CALA326
CASP338
CSER343
CTHR344
CSER345
CPHE354
CHOH601
AASN234
CHOH607
CTHR273
CTYR277
CASN281
CARG285
CARG319
CGLY320
CTHR321

site_idAC2
Number of Residues4
Detailsbinding site for residue MPD C 502
ChainResidue
AARG224
CGLY274
CILE275
CTYR376

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 Residues4
DetailsSITE: Interaction with phosphoserine on interacting protein => ECO:0000250
ChainResidueDetails
AARG58
AARG129
BARG58
BARG129

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate => ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS5
BLYS5

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS51
BLYS51

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CQV8
ChainResidueDetails
ASER60
BSER60

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS70
ALYS117
BLYS70
BLYS117

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q9CQV8
ChainResidueDetails
ATYR84
ATYR106
BTYR84
BTYR106

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68251
ChainResidueDetails
ASER186
BSER186

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER232
BSER232

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P27348
ChainResidueDetails
ALYS51
BLYS51

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PDB entries from 2024-05-01

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