5F74
Crystal structure of ChREBP:14-3-3 complex bound with AMP
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 | 0005829 | cellular_component | cytosol |
| A | 0006605 | biological_process | protein targeting |
| 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 | 0045184 | biological_process | establishment of protein localization |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue AMP A 301 |
| Chain | Residue |
| A | SER47 |
| B | ARG128 |
| A | LYS51 |
| A | ARG58 |
| A | LYS122 |
| A | ARG129 |
| A | TYR130 |
| A | ASN175 |
| B | ASN124 |
| B | TRP127 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9NP71 |
| Chain | Residue | Details |
| B | SER20 | |
| B | SER196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| B | SER23 | |
| B | SER25 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| B | THR27 |
| 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:0000269|PubMed:9705322 |
| Chain | Residue | Details |
| A | SER60 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P31946 |
| Chain | Residue | Details |
| A | LYS70 | |
| A | LYS117 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0007744|PubMed:16800626 |
| 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:0000250|UniProtKB:P31946 |
| 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 |
