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 | 0007165 | biological_process | signal transduction |
| A | 0008039 | biological_process | synaptic target recognition |
| A | 0008104 | biological_process | intracellular protein localization |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0019903 | molecular_function | protein phosphatase 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 | 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 | 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 | 0007165 | biological_process | signal transduction |
| B | 0008039 | biological_process | synaptic target recognition |
| B | 0008104 | biological_process | intracellular protein localization |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0019903 | molecular_function | protein phosphatase 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 | 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 | 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 | 4 |
| Details | Site: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"UniProtKB","id":"P63103","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA and PKB/AKT1","evidences":[{"source":"PubMed","id":"11956222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12865427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15883165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16376338","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by MAPK8","evidences":[{"source":"PubMed","id":"15071501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15696159","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63102","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Potts A.","Barblan J.","Claeys D.","Quadroni M."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19172738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
