5EXA
Small-molecule stabilization of the 14-3-3/Gab2 PPI interface
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
A | 0001525 | biological_process | angiogenesis |
A | 0003016 | biological_process | respiratory system process |
A | 0003723 | molecular_function | RNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005615 | cellular_component | extracellular space |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005925 | cellular_component | focal adhesion |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006605 | biological_process | protein targeting |
A | 0007165 | biological_process | signal transduction |
A | 0008039 | biological_process | synaptic target recognition |
A | 0008104 | biological_process | protein localization |
A | 0019901 | molecular_function | protein kinase binding |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0030324 | biological_process | lung development |
A | 0031625 | molecular_function | ubiquitin protein ligase binding |
A | 0031647 | biological_process | regulation of protein stability |
A | 0031982 | cellular_component | vesicle |
A | 0035148 | biological_process | tube formation |
A | 0042149 | biological_process | cellular response to glucose starvation |
A | 0042470 | cellular_component | melanosome |
A | 0042802 | molecular_function | identical protein binding |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0043067 | biological_process | regulation of programmed cell death |
A | 0044325 | molecular_function | transmembrane transporter binding |
A | 0045296 | molecular_function | cadherin binding |
A | 0045824 | biological_process | negative regulation of innate immune response |
A | 0050815 | molecular_function | phosphoserine residue binding |
A | 0051683 | biological_process | establishment of Golgi localization |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070371 | biological_process | ERK1 and ERK2 cascade |
A | 0070372 | biological_process | regulation of ERK1 and ERK2 cascade |
A | 0072562 | cellular_component | blood microparticle |
A | 0090128 | biological_process | regulation of synapse maturation |
A | 0090168 | biological_process | Golgi reassembly |
A | 0098686 | cellular_component | hippocampal mossy fiber to CA3 synapse |
A | 0098978 | cellular_component | glutamatergic synapse |
A | 0140297 | molecular_function | DNA-binding transcription factor binding |
A | 0140311 | molecular_function | protein sequestering activity |
A | 1900181 | biological_process | negative regulation of protein localization to nucleus |
A | 1904262 | biological_process | negative regulation of TORC1 signaling |
B | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
B | 0001525 | biological_process | angiogenesis |
B | 0003016 | biological_process | respiratory system process |
B | 0003723 | molecular_function | RNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005615 | cellular_component | extracellular space |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005925 | cellular_component | focal adhesion |
B | 0006468 | biological_process | protein phosphorylation |
B | 0006605 | biological_process | protein targeting |
B | 0007165 | biological_process | signal transduction |
B | 0008039 | biological_process | synaptic target recognition |
B | 0008104 | biological_process | protein localization |
B | 0019901 | molecular_function | protein kinase binding |
B | 0019904 | molecular_function | protein domain specific binding |
B | 0030324 | biological_process | lung development |
B | 0031625 | molecular_function | ubiquitin protein ligase binding |
B | 0031647 | biological_process | regulation of protein stability |
B | 0031982 | cellular_component | vesicle |
B | 0035148 | biological_process | tube formation |
B | 0042149 | biological_process | cellular response to glucose starvation |
B | 0042470 | cellular_component | melanosome |
B | 0042802 | molecular_function | identical protein binding |
B | 0043066 | biological_process | negative regulation of apoptotic process |
B | 0043067 | biological_process | regulation of programmed cell death |
B | 0044325 | molecular_function | transmembrane transporter binding |
B | 0045296 | molecular_function | cadherin binding |
B | 0045824 | biological_process | negative regulation of innate immune response |
B | 0050815 | molecular_function | phosphoserine residue binding |
B | 0051683 | biological_process | establishment of Golgi localization |
B | 0070062 | cellular_component | extracellular exosome |
B | 0070371 | biological_process | ERK1 and ERK2 cascade |
B | 0070372 | biological_process | regulation of ERK1 and ERK2 cascade |
B | 0072562 | cellular_component | blood microparticle |
B | 0090128 | biological_process | regulation of synapse maturation |
B | 0090168 | biological_process | Golgi reassembly |
B | 0098686 | cellular_component | hippocampal mossy fiber to CA3 synapse |
B | 0098978 | cellular_component | glutamatergic synapse |
B | 0140297 | molecular_function | DNA-binding transcription factor binding |
B | 0140311 | molecular_function | protein sequestering activity |
B | 1900181 | biological_process | negative regulation of protein localization to nucleus |
B | 1904262 | biological_process | negative regulation of TORC1 signaling |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue 5SO A 301 |
Chain | Residue |
A | PHE117 |
A | LYS120 |
A | PRO165 |
A | ASP213 |
D | PRO393 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG B 301 |
Chain | Residue |
B | THR205 |
B | GLN161 |
B | PRO162 |
B | THR163 |
B | GLU202 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue 5SO B 302 |
Chain | Residue |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | ASP213 |
C | LEU392 |
C | PRO393 |
site_id | AC4 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AC5 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AC6 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AC8 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
site_id | AC9 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD1 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD2 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD3 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD4 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD5 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD6 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD7 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD8 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AD9 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AE1 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
site_id | AE2 |
Number of Residues | 18 |
Details | binding site for residues BEZ A 302 and BEZ B 303 |
Chain | Residue |
A | PHE196 |
A | PHE196 |
A | MET218 |
A | ARG222 |
A | ARG222 |
B | ASN42 |
B | PHE117 |
B | LYS120 |
B | PRO165 |
B | PHE196 |
B | PHE196 |
B | ASP213 |
B | MET218 |
B | MET218 |
B | ARG222 |
B | ARG222 |
C | LEU392 |
C | PRO393 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:19172738, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | TPO391 | |
D | TPO391 | |
B | ARG56 | |
B | ARG127 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS3 | |
A | LYS68 | |
B | LYS3 | |
B | LYS68 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338 |
Chain | Residue | Details |
A | SER58 | |
B | SER58 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159 |
Chain | Residue | Details |
A | SER184 | |
B | SER184 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER207 | |
B | SER207 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63102 |
Chain | Residue | Details |
A | SER210 | |
B | SER210 |