6DHK
Bovine glutamate dehydrogenase complexed with ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| G | 0006520 | biological_process | amino acid metabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| H | 0006520 | biological_process | amino acid metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| I | 0006520 | biological_process | amino acid metabolic process |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| J | 0006520 | biological_process | amino acid metabolic process |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| K | 0006520 | biological_process | amino acid metabolic process |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| L | 0006520 | biological_process | amino acid metabolic process |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue ADP A 601 |
| Chain | Residue |
| A | HIS85 |
| B | LYS387 |
| B | SER393 |
| B | ARG396 |
| A | ARG86 |
| A | CYS115 |
| A | ALA116 |
| A | ASP119 |
| A | VAL120 |
| A | ARG491 |
| A | VAL492 |
| B | HIS209 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue ADP B 601 |
| Chain | Residue |
| B | HIS85 |
| B | ARG86 |
| B | ASP119 |
| B | VAL120 |
| B | PRO121 |
| B | PHE122 |
| B | ARG459 |
| B | LYS488 |
| B | VAL489 |
| B | VAL492 |
| F | HIS209 |
| F | LYS387 |
| F | SER393 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue ADP C 601 |
| Chain | Residue |
| C | HIS85 |
| C | ARG86 |
| C | ASP119 |
| C | VAL120 |
| C | PHE122 |
| C | ARG459 |
| C | LYS488 |
| D | ILE203 |
| D | HIS209 |
| D | LYS387 |
| D | SER393 |
| D | ARG396 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue ADP C 602 |
| Chain | Residue |
| C | ILE203 |
| C | HIS209 |
| C | LYS387 |
| C | SER393 |
| C | ARG396 |
| E | HIS85 |
| E | ARG86 |
| E | ALA116 |
| E | ASP119 |
| E | VAL120 |
| E | LYS488 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue ADP D 601 |
| Chain | Residue |
| D | HIS85 |
| D | ARG86 |
| D | ALA116 |
| D | ASP119 |
| D | VAL120 |
| D | ARG459 |
| D | LYS488 |
| D | VAL492 |
| E | ILE203 |
| E | HIS209 |
| E | LYS387 |
| E | SER393 |
| E | ARG396 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue ADP F 601 |
| Chain | Residue |
| A | ILE203 |
| A | HIS209 |
| A | LYS387 |
| A | SER393 |
| A | ARG396 |
| F | HIS85 |
| F | ARG86 |
| F | ASP119 |
| F | VAL120 |
| F | ARG459 |
| F | LYS488 |
| F | VAL492 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue ADP G 601 |
| Chain | Residue |
| G | HIS85 |
| G | ARG86 |
| G | ALA116 |
| G | ASP119 |
| G | VAL120 |
| G | ARG459 |
| G | LYS488 |
| G | VAL492 |
| H | ILE203 |
| H | HIS209 |
| H | LYS387 |
| H | SER393 |
| H | ARG396 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue ADP H 601 |
| Chain | Residue |
| L | ARG396 |
| H | HIS85 |
| H | ARG86 |
| H | ASP119 |
| H | VAL120 |
| H | PHE122 |
| H | ARG459 |
| H | LYS488 |
| H | VAL489 |
| H | VAL492 |
| L | ILE203 |
| L | HIS209 |
| L | LYS387 |
| L | SER393 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue ADP I 601 |
| Chain | Residue |
| I | HIS85 |
| I | ARG86 |
| I | ASP119 |
| I | VAL120 |
| I | ARG459 |
| I | LYS488 |
| I | VAL489 |
| I | VAL492 |
| J | ILE203 |
| J | HIS209 |
| J | LYS387 |
| J | SER393 |
| J | ARG396 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue ADP J 601 |
| Chain | Residue |
| J | HIS85 |
| J | ARG86 |
| J | ALA116 |
| J | ASP119 |
| J | VAL120 |
| J | ARG459 |
| J | LYS488 |
| J | VAL492 |
| K | HIS209 |
| K | LYS387 |
| K | SER393 |
| K | ARG396 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue ADP K 601 |
| Chain | Residue |
| I | ILE203 |
| I | HIS209 |
| I | LYS387 |
| I | SER393 |
| I | ARG396 |
| K | HIS85 |
| K | ARG86 |
| K | ALA116 |
| K | ASP119 |
| K | VAL120 |
| K | PHE122 |
| K | ARG459 |
| K | LYS488 |
| K | VAL492 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for residue ADP L 601 |
| Chain | Residue |
| G | ILE203 |
| G | HIS209 |
| G | LYS387 |
| G | SER393 |
| G | ARG396 |
| L | HIS85 |
| L | ARG86 |
| L | ALA116 |
| L | ASP119 |
| L | VAL120 |
| L | PHE122 |
| L | ARG459 |
| L | LYS488 |
| L | VAL492 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. VpfGGAKaGvkiNP |
| Chain | Residue | Details |
| A | VAL120-PRO133 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10011 |
| Chain | Residue | Details |
| A | LYS126 | |
| J | LYS126 | |
| K | LYS126 | |
| L | LYS126 | |
| B | LYS126 | |
| C | LYS126 | |
| D | LYS126 | |
| E | LYS126 | |
| F | LYS126 | |
| G | LYS126 | |
| H | LYS126 | |
| I | LYS126 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 132 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11254391 |
| Chain | Residue | Details |
| A | GLN84 | |
| A | SER381 | |
| J | GLN84 | |
| J | LYS90 | |
| J | LYS114 | |
| J | ASP119 | |
| J | HIS195 | |
| J | HIS209 | |
| J | SER213 | |
| J | TYR262 | |
| J | ARG265 | |
| J | SER381 | |
| A | LYS387 | |
| J | LYS387 | |
| K | GLN84 | |
| K | LYS90 | |
| K | LYS114 | |
| K | ASP119 | |
| K | HIS195 | |
| K | HIS209 | |
| K | SER213 | |
| K | TYR262 | |
| K | ARG265 | |
| B | GLN84 | |
| K | SER381 | |
| K | LYS387 | |
| L | GLN84 | |
| L | LYS90 | |
| L | LYS114 | |
| L | ASP119 | |
| L | HIS195 | |
| L | HIS209 | |
| L | SER213 | |
| L | TYR262 | |
| B | LYS90 | |
| L | ARG265 | |
| L | SER381 | |
| L | LYS387 | |
| B | LYS114 | |
| B | ASP119 | |
| B | HIS195 | |
| B | HIS209 | |
| B | SER213 | |
| B | TYR262 | |
| A | LYS90 | |
| B | ARG265 | |
| B | SER381 | |
| B | LYS387 | |
| C | GLN84 | |
| C | LYS90 | |
| C | LYS114 | |
| C | ASP119 | |
| C | HIS195 | |
| C | HIS209 | |
| C | SER213 | |
| A | LYS114 | |
| C | TYR262 | |
| C | ARG265 | |
| C | SER381 | |
| C | LYS387 | |
| D | GLN84 | |
| D | LYS90 | |
| D | LYS114 | |
| D | ASP119 | |
| D | HIS195 | |
| D | HIS209 | |
| A | ASP119 | |
| D | SER213 | |
| D | TYR262 | |
| D | ARG265 | |
| D | SER381 | |
| D | LYS387 | |
| E | GLN84 | |
| E | LYS90 | |
| E | LYS114 | |
| E | ASP119 | |
| E | HIS195 | |
| A | HIS195 | |
| E | HIS209 | |
| E | SER213 | |
| E | TYR262 | |
| E | ARG265 | |
| E | SER381 | |
| E | LYS387 | |
| F | GLN84 | |
| F | LYS90 | |
| F | LYS114 | |
| F | ASP119 | |
| A | HIS209 | |
| F | HIS195 | |
| F | HIS209 | |
| F | SER213 | |
| F | TYR262 | |
| F | ARG265 | |
| F | SER381 | |
| F | LYS387 | |
| G | GLN84 | |
| G | LYS90 | |
| G | LYS114 | |
| A | SER213 | |
| G | ASP119 | |
| G | HIS195 | |
| G | HIS209 | |
| G | SER213 | |
| G | TYR262 | |
| G | ARG265 | |
| G | SER381 | |
| G | LYS387 | |
| H | GLN84 | |
| H | LYS90 | |
| A | TYR262 | |
| H | LYS114 | |
| H | ASP119 | |
| H | HIS195 | |
| H | HIS209 | |
| H | SER213 | |
| H | TYR262 | |
| H | ARG265 | |
| H | SER381 | |
| H | LYS387 | |
| I | GLN84 | |
| A | ARG265 | |
| I | LYS90 | |
| I | LYS114 | |
| I | ASP119 | |
| I | HIS195 | |
| I | HIS209 | |
| I | SER213 | |
| I | TYR262 | |
| I | ARG265 | |
| I | SER381 | |
| I | LYS387 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12653548 |
| Chain | Residue | Details |
| A | SER393 | |
| E | ARG459 | |
| F | SER393 | |
| F | ARG459 | |
| G | SER393 | |
| G | ARG459 | |
| H | SER393 | |
| H | ARG459 | |
| I | SER393 | |
| I | ARG459 | |
| J | SER393 | |
| A | ARG459 | |
| J | ARG459 | |
| K | SER393 | |
| K | ARG459 | |
| L | SER393 | |
| L | ARG459 | |
| B | SER393 | |
| B | ARG459 | |
| C | SER393 | |
| C | ARG459 | |
| D | SER393 | |
| D | ARG459 | |
| E | SER393 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | LYS11 | |
| E | LYS143 | |
| F | LYS11 | |
| F | LYS143 | |
| G | LYS11 | |
| G | LYS143 | |
| H | LYS11 | |
| H | LYS143 | |
| I | LYS11 | |
| I | LYS143 | |
| J | LYS11 | |
| A | LYS143 | |
| J | LYS143 | |
| K | LYS11 | |
| K | LYS143 | |
| L | LYS11 | |
| L | LYS143 | |
| B | LYS11 | |
| B | LYS143 | |
| C | LYS11 | |
| C | LYS143 | |
| D | LYS11 | |
| D | LYS143 | |
| E | LYS11 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | SER22 | |
| E | SER71 | |
| F | SER22 | |
| F | SER71 | |
| G | SER22 | |
| G | SER71 | |
| H | SER22 | |
| H | SER71 | |
| I | SER22 | |
| I | SER71 | |
| J | SER22 | |
| A | SER71 | |
| J | SER71 | |
| K | SER22 | |
| K | SER71 | |
| L | SER22 | |
| L | SER71 | |
| B | SER22 | |
| B | SER71 | |
| C | SER22 | |
| C | SER71 | |
| D | SER22 | |
| D | SER71 | |
| E | SER22 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 108 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22076378 |
| Chain | Residue | Details |
| A | LYS27 | |
| B | LYS27 | |
| L | LYS27 | |
| L | LYS53 | |
| L | LYS105 | |
| L | LYS306 | |
| L | LYS358 | |
| L | LYS400 | |
| L | LYS446 | |
| L | LYS470 | |
| L | LYS488 | |
| B | LYS53 | |
| B | LYS105 | |
| B | LYS306 | |
| B | LYS358 | |
| B | LYS400 | |
| B | LYS446 | |
| B | LYS470 | |
| B | LYS488 | |
| C | LYS27 | |
| A | LYS53 | |
| C | LYS53 | |
| C | LYS105 | |
| C | LYS306 | |
| C | LYS358 | |
| C | LYS400 | |
| C | LYS446 | |
| C | LYS470 | |
| C | LYS488 | |
| D | LYS27 | |
| D | LYS53 | |
| A | LYS105 | |
| D | LYS105 | |
| D | LYS306 | |
| D | LYS358 | |
| D | LYS400 | |
| D | LYS446 | |
| D | LYS470 | |
| D | LYS488 | |
| E | LYS27 | |
| E | LYS53 | |
| E | LYS105 | |
| A | LYS306 | |
| E | LYS306 | |
| E | LYS358 | |
| E | LYS400 | |
| E | LYS446 | |
| E | LYS470 | |
| E | LYS488 | |
| F | LYS27 | |
| F | LYS53 | |
| F | LYS105 | |
| F | LYS306 | |
| A | LYS358 | |
| F | LYS358 | |
| F | LYS400 | |
| F | LYS446 | |
| F | LYS470 | |
| F | LYS488 | |
| G | LYS27 | |
| G | LYS53 | |
| G | LYS105 | |
| G | LYS306 | |
| G | LYS358 | |
| A | LYS400 | |
| G | LYS400 | |
| G | LYS446 | |
| G | LYS470 | |
| G | LYS488 | |
| H | LYS27 | |
| H | LYS53 | |
| H | LYS105 | |
| H | LYS306 | |
| H | LYS358 | |
| H | LYS400 | |
| A | LYS446 | |
| H | LYS446 | |
| H | LYS470 | |
| H | LYS488 | |
| I | LYS27 | |
| I | LYS53 | |
| I | LYS105 | |
| I | LYS306 | |
| I | LYS358 | |
| I | LYS400 | |
| I | LYS446 | |
| A | LYS470 | |
| I | LYS470 | |
| I | LYS488 | |
| J | LYS27 | |
| J | LYS53 | |
| J | LYS105 | |
| J | LYS306 | |
| J | LYS358 | |
| J | LYS400 | |
| J | LYS446 | |
| J | LYS470 | |
| A | LYS488 | |
| J | LYS488 | |
| K | LYS27 | |
| K | LYS53 | |
| K | LYS105 | |
| K | LYS306 | |
| K | LYS358 | |
| K | LYS400 | |
| K | LYS446 | |
| K | LYS470 | |
| K | LYS488 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 36 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22076378 |
| Chain | Residue | Details |
| A | LYS33 | |
| D | LYS33 | |
| D | LYS329 | |
| D | LYS342 | |
| E | LYS33 | |
| E | LYS329 | |
| E | LYS342 | |
| F | LYS33 | |
| F | LYS329 | |
| F | LYS342 | |
| G | LYS33 | |
| A | LYS329 | |
| G | LYS329 | |
| G | LYS342 | |
| H | LYS33 | |
| H | LYS329 | |
| H | LYS342 | |
| I | LYS33 | |
| I | LYS329 | |
| I | LYS342 | |
| J | LYS33 | |
| J | LYS329 | |
| A | LYS342 | |
| J | LYS342 | |
| K | LYS33 | |
| K | LYS329 | |
| K | LYS342 | |
| L | LYS33 | |
| L | LYS329 | |
| L | LYS342 | |
| B | LYS33 | |
| B | LYS329 | |
| B | LYS342 | |
| C | LYS33 | |
| C | LYS329 | |
| C | LYS342 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | TYR78 | |
| J | TYR78 | |
| K | TYR78 | |
| L | TYR78 | |
| B | TYR78 | |
| C | TYR78 | |
| D | TYR78 | |
| E | TYR78 | |
| F | TYR78 | |
| G | TYR78 | |
| H | TYR78 | |
| I | TYR78 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | LYS90 | |
| J | LYS90 | |
| K | LYS90 | |
| L | LYS90 | |
| B | LYS90 | |
| C | LYS90 | |
| D | LYS90 | |
| E | LYS90 | |
| F | LYS90 | |
| G | LYS90 | |
| H | LYS90 | |
| I | LYS90 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 48 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | LYS114 | |
| C | LYS130 | |
| C | LYS154 | |
| C | LYS269 | |
| D | LYS114 | |
| D | LYS130 | |
| D | LYS154 | |
| D | LYS269 | |
| E | LYS114 | |
| E | LYS130 | |
| E | LYS154 | |
| A | LYS130 | |
| E | LYS269 | |
| F | LYS114 | |
| F | LYS130 | |
| F | LYS154 | |
| F | LYS269 | |
| G | LYS114 | |
| G | LYS130 | |
| G | LYS154 | |
| G | LYS269 | |
| H | LYS114 | |
| A | LYS154 | |
| H | LYS130 | |
| H | LYS154 | |
| H | LYS269 | |
| I | LYS114 | |
| I | LYS130 | |
| I | LYS154 | |
| I | LYS269 | |
| J | LYS114 | |
| J | LYS130 | |
| J | LYS154 | |
| A | LYS269 | |
| J | LYS269 | |
| K | LYS114 | |
| K | LYS130 | |
| K | LYS154 | |
| K | LYS269 | |
| L | LYS114 | |
| L | LYS130 | |
| L | LYS154 | |
| L | LYS269 | |
| B | LYS114 | |
| B | LYS130 | |
| B | LYS154 | |
| B | LYS269 | |
| C | LYS114 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | MOD_RES: ADP-ribosylcysteine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | CYS115 | |
| J | CYS115 | |
| K | CYS115 | |
| L | CYS115 | |
| B | CYS115 | |
| C | CYS115 | |
| D | CYS115 | |
| E | CYS115 | |
| F | CYS115 | |
| G | CYS115 | |
| H | CYS115 | |
| I | CYS115 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 96 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | LYS126 | |
| B | LYS134 | |
| B | LYS289 | |
| B | LYS295 | |
| B | LYS308 | |
| B | LYS333 | |
| B | LYS420 | |
| B | LYS423 | |
| C | LYS126 | |
| C | LYS134 | |
| C | LYS289 | |
| A | LYS134 | |
| C | LYS295 | |
| C | LYS308 | |
| C | LYS333 | |
| C | LYS420 | |
| C | LYS423 | |
| D | LYS126 | |
| D | LYS134 | |
| D | LYS289 | |
| D | LYS295 | |
| D | LYS308 | |
| A | LYS289 | |
| D | LYS333 | |
| D | LYS420 | |
| D | LYS423 | |
| E | LYS126 | |
| E | LYS134 | |
| E | LYS289 | |
| E | LYS295 | |
| E | LYS308 | |
| E | LYS333 | |
| E | LYS420 | |
| A | LYS295 | |
| E | LYS423 | |
| F | LYS126 | |
| F | LYS134 | |
| F | LYS289 | |
| F | LYS295 | |
| F | LYS308 | |
| F | LYS333 | |
| F | LYS420 | |
| F | LYS423 | |
| G | LYS126 | |
| A | LYS308 | |
| G | LYS134 | |
| G | LYS289 | |
| G | LYS295 | |
| G | LYS308 | |
| G | LYS333 | |
| G | LYS420 | |
| G | LYS423 | |
| H | LYS126 | |
| H | LYS134 | |
| H | LYS289 | |
| A | LYS333 | |
| H | LYS295 | |
| H | LYS308 | |
| H | LYS333 | |
| H | LYS420 | |
| H | LYS423 | |
| I | LYS126 | |
| I | LYS134 | |
| I | LYS289 | |
| I | LYS295 | |
| I | LYS308 | |
| A | LYS420 | |
| I | LYS333 | |
| I | LYS420 | |
| I | LYS423 | |
| J | LYS126 | |
| J | LYS134 | |
| J | LYS289 | |
| J | LYS295 | |
| J | LYS308 | |
| J | LYS333 | |
| J | LYS420 | |
| A | LYS423 | |
| J | LYS423 | |
| K | LYS126 | |
| K | LYS134 | |
| K | LYS289 | |
| K | LYS295 | |
| K | LYS308 | |
| K | LYS333 | |
| K | LYS420 | |
| K | LYS423 | |
| L | LYS126 | |
| B | LYS126 | |
| L | LYS134 | |
| L | LYS289 | |
| L | LYS295 | |
| L | LYS308 | |
| L | LYS333 | |
| L | LYS420 | |
| L | LYS423 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 24 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | SER170 | |
| E | SER327 | |
| F | SER170 | |
| F | SER327 | |
| G | SER170 | |
| G | SER327 | |
| H | SER170 | |
| H | SER327 | |
| I | SER170 | |
| I | SER327 | |
| J | SER170 | |
| A | SER327 | |
| J | SER327 | |
| K | SER170 | |
| K | SER327 | |
| L | SER170 | |
| L | SER327 | |
| B | SER170 | |
| B | SER327 | |
| C | SER170 | |
| C | SER327 | |
| D | SER170 | |
| D | SER327 | |
| E | SER170 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10860 |
| Chain | Residue | Details |
| A | THR353 | |
| J | THR353 | |
| K | THR353 | |
| L | THR353 | |
| B | THR353 | |
| C | THR353 | |
| D | THR353 | |
| E | THR353 | |
| F | THR353 | |
| G | THR353 | |
| H | THR353 | |
| I | THR353 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | TYR455 | |
| J | TYR455 | |
| K | TYR455 | |
| L | TYR455 | |
| B | TYR455 | |
| C | TYR455 | |
| D | TYR455 | |
| E | TYR455 | |
| F | TYR455 | |
| G | TYR455 | |
| H | TYR455 | |
| I | TYR455 |
