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6GNN

Exoenzyme T from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form bound to STO1101

Functional Information from GO Data
ChainGOidnamespacecontents
A0004860molecular_functionprotein kinase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
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_processobsolete negative 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
C0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue F4W C 501
ChainResidue
CTYR277
CGLU382
CASN281
CARG285
CARG319
CGLY320
CSER343
CTHR344
CSER345
CGLU380

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 Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340
ChainResidueDetails
CARG319
CSER343
CGLU382

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate => ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
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:0000250|UniProtKB:Q9CQV8
ChainResidueDetails
ASER60

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS70
ALYS117

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q9CQV8
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:0007744|PubMed:24275569
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

226707

PDB entries from 2024-10-30

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