1NQT
Crystal structure of bovine Glutamate dehydrogenase-ADP complex
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 1 |
Chain | Residue |
A | GLN85 |
B | LYS387 |
B | SER393 |
B | ARG396 |
A | ARG86 |
A | ALA116 |
A | ASP119 |
A | VAL120 |
A | ARG459 |
A | VAL492 |
B | ILE203 |
B | HIS209 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP B 2 |
Chain | Residue |
B | GLN85 |
B | ARG86 |
B | ALA116 |
B | ASP119 |
B | VAL120 |
B | ARG459 |
B | LYS488 |
B | VAL489 |
B | VAL492 |
F | ILE203 |
F | HIS209 |
F | LYS387 |
F | SER393 |
F | ARG396 |
F | GLU445 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP C 3 |
Chain | Residue |
C | GLN85 |
C | ARG86 |
C | ALA116 |
C | ASP119 |
C | VAL120 |
C | ARG459 |
C | LYS488 |
C | VAL492 |
D | ILE203 |
D | LYS387 |
D | SER393 |
D | ARG396 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP D 4 |
Chain | Residue |
D | GLN85 |
D | ARG86 |
D | CYS115 |
D | ALA116 |
D | ASP119 |
D | VAL120 |
D | ARG459 |
D | VAL492 |
E | ILE203 |
E | HIS209 |
E | LYS387 |
E | SER393 |
E | ARG396 |
E | GLU445 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADP E 5 |
Chain | Residue |
C | ILE203 |
C | LYS387 |
C | SER393 |
C | ARG396 |
E | GLN85 |
E | ARG86 |
E | ALA116 |
E | ASP119 |
E | VAL120 |
E | ARG459 |
E | LYS488 |
E | VAL489 |
E | VAL492 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADP F 502 |
Chain | Residue |
A | ILE203 |
A | HIS209 |
A | LYS387 |
A | SER393 |
A | ARG396 |
F | GLN85 |
F | ARG86 |
F | ALA116 |
F | ASP119 |
F | VAL120 |
F | ARG459 |
F | LYS488 |
F | VAL492 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP G 502 |
Chain | Residue |
G | GLN85 |
G | ARG86 |
G | ALA116 |
G | ASP119 |
G | ARG459 |
G | LYS488 |
G | VAL492 |
H | ILE203 |
H | HIS209 |
H | LYS387 |
H | SER393 |
H | ARG396 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ADP H 502 |
Chain | Residue |
L | LYS387 |
L | SER393 |
L | ARG396 |
H | GLN85 |
H | ARG86 |
H | ASP119 |
H | ARG459 |
H | LYS488 |
H | VAL489 |
L | ILE203 |
L | HIS209 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP I 502 |
Chain | Residue |
I | GLN85 |
I | ARG86 |
I | ALA116 |
I | ASP119 |
I | VAL120 |
I | ARG459 |
I | LYS488 |
I | VAL489 |
I | VAL492 |
J | ILE203 |
J | HIS209 |
J | LYS387 |
J | SER393 |
J | ARG396 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP J 502 |
Chain | Residue |
J | GLN85 |
J | ARG86 |
J | ALA116 |
J | ASP119 |
J | VAL120 |
J | ARG459 |
J | LYS488 |
K | ILE203 |
K | HIS209 |
K | LYS387 |
K | SER393 |
K | ARG396 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP K 502 |
Chain | Residue |
I | ILE203 |
I | HIS209 |
I | LYS387 |
I | SER393 |
I | ARG396 |
K | GLN85 |
K | ARG86 |
K | ASP119 |
K | VAL120 |
K | PRO121 |
K | PHE122 |
K | ARG459 |
K | LYS488 |
K | VAL492 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADP L 502 |
Chain | Residue |
G | ILE203 |
G | HIS209 |
G | LYS387 |
G | SER393 |
G | ARG396 |
L | GLN85 |
L | ARG86 |
L | ALA116 |
L | ASP119 |
L | VAL120 |
L | PHE122 |
L | ARG459 |
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 | HIS84 | |
A | SER381 | |
J | HIS84 | |
J | LYS90 | |
J | LYS114 | |
J | ASP119 | |
J | HIS195 | |
J | HIS209 | |
J | SER213 | |
J | TYR262 | |
J | ARG265 | |
J | SER381 | |
A | LYS387 | |
J | LYS387 | |
K | HIS84 | |
K | LYS90 | |
K | LYS114 | |
K | ASP119 | |
K | HIS195 | |
K | HIS209 | |
K | SER213 | |
K | TYR262 | |
K | ARG265 | |
B | HIS84 | |
K | SER381 | |
K | LYS387 | |
L | HIS84 | |
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 | HIS84 | |
C | LYS90 | |
C | LYS114 | |
C | ASP119 | |
C | HIS195 | |
C | HIS209 | |
C | SER213 | |
A | LYS114 | |
C | TYR262 | |
C | ARG265 | |
C | SER381 | |
C | LYS387 | |
D | HIS84 | |
D | LYS90 | |
D | LYS114 | |
D | ASP119 | |
D | HIS195 | |
D | HIS209 | |
A | ASP119 | |
D | SER213 | |
D | TYR262 | |
D | ARG265 | |
D | SER381 | |
D | LYS387 | |
E | HIS84 | |
E | LYS90 | |
E | LYS114 | |
E | ASP119 | |
E | HIS195 | |
A | HIS195 | |
E | HIS209 | |
E | SER213 | |
E | TYR262 | |
E | ARG265 | |
E | SER381 | |
E | LYS387 | |
F | HIS84 | |
F | LYS90 | |
F | LYS114 | |
F | ASP119 | |
A | HIS209 | |
F | HIS195 | |
F | HIS209 | |
F | SER213 | |
F | TYR262 | |
F | ARG265 | |
F | SER381 | |
F | LYS387 | |
G | HIS84 | |
G | LYS90 | |
G | LYS114 | |
A | SER213 | |
G | ASP119 | |
G | HIS195 | |
G | HIS209 | |
G | SER213 | |
G | TYR262 | |
G | ARG265 | |
G | SER381 | |
G | LYS387 | |
H | HIS84 | |
H | LYS90 | |
A | TYR262 | |
H | LYS114 | |
H | ASP119 | |
H | HIS195 | |
H | HIS209 | |
H | SER213 | |
H | TYR262 | |
H | ARG265 | |
H | SER381 | |
H | LYS387 | |
I | HIS84 | |
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 | ARG33 | |
D | ARG33 | |
D | LYS329 | |
D | LYS342 | |
E | ARG33 | |
E | LYS329 | |
E | LYS342 | |
F | ARG33 | |
F | LYS329 | |
F | LYS342 | |
G | ARG33 | |
A | LYS329 | |
G | LYS329 | |
G | LYS342 | |
H | ARG33 | |
H | LYS329 | |
H | LYS342 | |
I | ARG33 | |
I | LYS329 | |
I | LYS342 | |
J | ARG33 | |
J | LYS329 | |
A | LYS342 | |
J | LYS342 | |
K | ARG33 | |
K | LYS329 | |
K | LYS342 | |
L | ARG33 | |
L | LYS329 | |
L | LYS342 | |
B | ARG33 | |
B | LYS329 | |
B | LYS342 | |
C | ARG33 | |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
A | LYS126 | |
A | ASP168 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
J | LYS126 | |
J | ASP168 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
K | LYS126 | |
K | ASP168 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
L | LYS126 | |
L | ASP168 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
B | LYS126 | |
B | ASP168 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
C | LYS126 | |
C | ASP168 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
D | LYS126 | |
D | ASP168 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
E | LYS126 | |
E | ASP168 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
F | LYS126 | |
F | ASP168 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
G | LYS126 | |
G | ASP168 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
H | LYS126 | |
H | ASP168 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
I | LYS126 | |
I | ASP168 |