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
Chain | GOid | namespace | contents |
A | 0004860 | molecular_function | protein kinase inhibitor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005773 | cellular_component | vacuole |
A | 0005774 | cellular_component | vacuolar membrane |
A | 0005829 | cellular_component | cytosol |
A | 0005925 | cellular_component | focal adhesion |
A | 0006605 | biological_process | protein targeting |
A | 0007165 | biological_process | signal transduction |
A | 0008104 | biological_process | protein localization |
A | 0016020 | cellular_component | membrane |
A | 0019899 | molecular_function | enzyme binding |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0035308 | biological_process | obsolete negative regulation of protein dephosphorylation |
A | 0042470 | cellular_component | melanosome |
A | 0042802 | molecular_function | identical protein binding |
A | 0042826 | molecular_function | histone deacetylase binding |
A | 0043085 | biological_process | positive regulation of catalytic activity |
A | 0045296 | molecular_function | cadherin binding |
A | 0045744 | biological_process | negative regulation of G protein-coupled receptor signaling pathway |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0050815 | molecular_function | phosphoserine residue binding |
A | 0051219 | molecular_function | phosphoprotein binding |
A | 0051220 | biological_process | cytoplasmic sequestering of protein |
A | 0070062 | cellular_component | extracellular exosome |
C | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue F4W C 501 |
Chain | Residue |
C | TYR277 |
C | GLU382 |
C | ASN281 |
C | ARG285 |
C | ARG319 |
C | GLY320 |
C | SER343 |
C | THR344 |
C | SER345 |
C | GLU380 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340 |
Chain | Residue | Details |
C | ARG319 | |
C | SER343 | |
C | GLU382 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate => ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | MET1 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR2 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27348 |
Chain | Residue | Details |
A | LYS5 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P27348 |
Chain | Residue | Details |
A | LYS51 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CQV8 |
Chain | Residue | Details |
A | SER60 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS70 | |
A | LYS117 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q9CQV8 |
Chain | Residue | Details |
A | TYR84 | |
A | TYR106 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68251 |
Chain | Residue | Details |
A | SER186 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER232 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P27348 |
Chain | Residue | Details |
A | LYS51 |