5JM4
Crystal structure of 14-3-3zeta in complex with a cyclic peptide involving an adamantyl and a dicarboxy side chain
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 | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| A | PHE196 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residues BEZ A 301 and BEZ B 301 |
| Chain | Residue |
| A | PHE196 |
| A | GLN219 |
| A | ARG222 |
| A | ARG222 |
| B | PHE196 |
| B | PHE196 |
| B | ARG222 |
| B | ARG222 |
| site_id | AE1 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide GLY D 421 and MKD D 422 |
| Chain | Residue |
| A | PRO165 |
| A | ASP213 |
| D | GLN420 |
| D | A1G423 |
| D | ASP424 |
| D | MKD425 |
| D | LEU426 |
| D | HOH504 |
| site_id | AE2 |
| Number of Residues | 9 |
| Details | binding site for residues MKD D 422 and A1G D 423 |
| Chain | Residue |
| A | PRO165 |
| A | ASP213 |
| D | GLN420 |
| D | GLY421 |
| D | ASP424 |
| D | MKD425 |
| D | LEU426 |
| D | LEU428 |
| D | HOH502 |
| site_id | AE3 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide A1G D 423 and ASP D 424 |
| Chain | Residue |
| A | LYS49 |
| D | GLN420 |
| D | GLY421 |
| D | MKD422 |
| D | MKD425 |
| D | LEU426 |
| D | ASP427 |
| D | LEU428 |
| D | HOH502 |
| site_id | AE4 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide ASP D 424 and MKD D 425 |
| Chain | Residue |
| A | ASN42 |
| A | SER45 |
| A | LYS49 |
| D | GLN420 |
| D | GLY421 |
| D | MKD422 |
| D | A1G423 |
| D | LEU426 |
| D | ASP427 |
| site_id | AE5 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide MKD D 425 and LEU D 426 |
| Chain | Residue |
| A | ASN42 |
| A | SER45 |
| A | LYS120 |
| A | PRO165 |
| D | GLY421 |
| D | MKD422 |
| D | A1G423 |
| D | ASP424 |
| D | ASP427 |
| D | LEU428 |
| site_id | AE6 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide ALA D 429 and 6L9 D 430 |
| Chain | Residue |
| A | ARG56 |
| A | ARG60 |
| A | ARG127 |
| A | ASN173 |
| A | VAL176 |
| D | LEU428 |
| D | HOH503 |
| site_id | AE7 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide GLY E 421 and MKD E 422 |
| Chain | Residue |
| B | PRO165 |
| B | ASP213 |
| E | GLN420 |
| E | A1G423 |
| E | ASP424 |
| E | MKD425 |
| E | LEU426 |
| site_id | AE8 |
| Number of Residues | 10 |
| Details | binding site for residues MKD E 422 and MKD E 425 |
| Chain | Residue |
| B | ASN42 |
| B | SER45 |
| B | VAL46 |
| B | PRO165 |
| B | ASP213 |
| E | GLY421 |
| E | A1G423 |
| E | ASP424 |
| E | LEU426 |
| E | ASP427 |
| site_id | AE9 |
| Number of Residues | 9 |
| Details | binding site for residues MKD E 422 and A1G E 423 |
| Chain | Residue |
| B | PRO165 |
| B | ASP213 |
| B | ILE217 |
| E | GLY421 |
| E | ASP424 |
| E | MKD425 |
| E | LEU426 |
| E | LEU428 |
| E | HOH502 |
| site_id | AF1 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide A1G E 423 and ASP E 424 |
| Chain | Residue |
| B | LYS49 |
| B | ASP213 |
| B | ILE217 |
| E | GLN420 |
| E | GLY421 |
| E | MKD422 |
| E | MKD425 |
| E | LEU426 |
| E | ASP427 |
| E | LEU428 |
| E | HOH501 |
| E | HOH502 |
| site_id | AF2 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide ASP E 424 and MKD E 425 |
| Chain | Residue |
| B | ASN42 |
| B | SER45 |
| B | VAL46 |
| B | LYS49 |
| E | GLN420 |
| E | GLY421 |
| E | MKD422 |
| E | A1G423 |
| E | LEU426 |
| E | ASP427 |
| E | HOH501 |
| site_id | AF3 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide MKD E 425 and LEU E 426 |
| Chain | Residue |
| B | ASN42 |
| B | SER45 |
| B | VAL46 |
| B | LYS120 |
| B | ILE217 |
| E | GLY421 |
| E | MKD422 |
| E | A1G423 |
| E | ASP424 |
| E | ASP427 |
| E | LEU428 |
| site_id | AF4 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide ALA E 429 and 6L9 E 430 |
| Chain | Residue |
| B | ARG56 |
| B | ARG60 |
| B | ARG127 |
| B | ASN173 |
| B | VAL176 |
| E | LEU428 |
| E | HOH505 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | SITE: Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 |
| Chain | Residue | Details |
| A | ARG56 | |
| A | ARG127 | |
| 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 |
