3ETD
Structure of glutamate dehydrogenase complexed with bithionol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| A | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| A | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006538 | biological_process | glutamate catabolic process |
| A | 0006541 | biological_process | glutamine 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 |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0072350 | biological_process | tricarboxylic acid metabolic process |
| B | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| B | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| B | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006538 | biological_process | glutamate catabolic process |
| B | 0006541 | biological_process | glutamine 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 |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0072350 | biological_process | tricarboxylic acid metabolic process |
| C | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| C | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| C | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006538 | biological_process | glutamate catabolic process |
| C | 0006541 | biological_process | glutamine 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 |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0072350 | biological_process | tricarboxylic acid metabolic process |
| D | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| D | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| D | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005525 | molecular_function | GTP binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005743 | cellular_component | mitochondrial inner membrane |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006538 | biological_process | glutamate catabolic process |
| D | 0006541 | biological_process | glutamine 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 |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0072350 | biological_process | tricarboxylic acid metabolic process |
| E | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| E | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| E | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005525 | molecular_function | GTP binding |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005743 | cellular_component | mitochondrial inner membrane |
| E | 0005783 | cellular_component | endoplasmic reticulum |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006538 | biological_process | glutamate catabolic process |
| E | 0006541 | biological_process | glutamine 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 |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0072350 | biological_process | tricarboxylic acid metabolic process |
| F | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
| F | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| F | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005525 | molecular_function | GTP binding |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005743 | cellular_component | mitochondrial inner membrane |
| F | 0005783 | cellular_component | endoplasmic reticulum |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0006538 | biological_process | glutamate catabolic process |
| F | 0006541 | biological_process | glutamine 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 |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0072350 | biological_process | tricarboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NDP A 551 |
| Chain | Residue |
| A | ARG94 |
| A | GLY253 |
| A | ASN254 |
| A | VAL255 |
| A | GLU275 |
| A | SER276 |
| A | ALA326 |
| A | GLY347 |
| A | ALA348 |
| A | ASN349 |
| A | ASN374 |
| A | LYS134 |
| A | GLU550 |
| A | ASP168 |
| A | MET169 |
| A | SER170 |
| A | ARG211 |
| A | THR215 |
| A | GLN250 |
| A | PHE252 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GTP A 553 |
| Chain | Residue |
| A | HIS209 |
| A | GLY210 |
| A | ILE212 |
| A | ARG217 |
| A | ARG261 |
| A | ARG265 |
| A | GLU292 |
| A | HIS450 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NDP B 551 |
| Chain | Residue |
| B | ASP168 |
| B | MET169 |
| B | SER170 |
| B | ARG211 |
| B | THR215 |
| B | GLN250 |
| B | PHE252 |
| B | GLY253 |
| B | ASN254 |
| B | VAL255 |
| B | GLU275 |
| B | SER276 |
| B | ALA326 |
| B | GLY347 |
| B | ALA348 |
| B | ASN349 |
| B | ASN374 |
| B | GLU550 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GTP B 553 |
| Chain | Residue |
| B | HIS209 |
| B | HIS258 |
| B | ARG261 |
| B | TYR262 |
| B | ARG265 |
| B | GLU292 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP C 551 |
| Chain | Residue |
| C | ARG94 |
| C | ASP168 |
| C | MET169 |
| C | SER170 |
| C | ARG211 |
| C | THR215 |
| C | GLN250 |
| C | PHE252 |
| C | GLY253 |
| C | ASN254 |
| C | VAL255 |
| C | GLU275 |
| C | SER276 |
| C | ALA326 |
| C | GLY347 |
| C | ASN349 |
| C | ASN374 |
| C | GLU550 |
| C | HOH556 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GTP C 553 |
| Chain | Residue |
| C | ILE212 |
| C | SER213 |
| C | ARG261 |
| C | TYR262 |
| C | ARG265 |
| C | GLU292 |
| C | LYS446 |
| C | HIS450 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP D 551 |
| Chain | Residue |
| D | ARG94 |
| D | ASP168 |
| D | MET169 |
| D | SER170 |
| D | ARG211 |
| D | THR215 |
| D | GLN250 |
| D | PHE252 |
| D | GLY253 |
| D | ASN254 |
| D | VAL255 |
| D | GLU275 |
| D | SER276 |
| D | ALA326 |
| D | GLY347 |
| D | ALA348 |
| D | ASN349 |
| D | ASN374 |
| D | GLU550 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GTP D 553 |
| Chain | Residue |
| D | GLY210 |
| D | ARG217 |
| D | ARG261 |
| D | TYR262 |
| D | ARG265 |
| D | GLU292 |
| D | HIS450 |
| D | HIS209 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP E 551 |
| Chain | Residue |
| E | LYS134 |
| E | PRO167 |
| E | ASP168 |
| E | MET169 |
| E | SER170 |
| E | ARG211 |
| E | THR215 |
| E | GLN250 |
| E | PHE252 |
| E | GLY253 |
| E | ASN254 |
| E | VAL255 |
| E | GLU275 |
| E | SER276 |
| E | ALA326 |
| E | GLY347 |
| E | ALA348 |
| E | ASN349 |
| E | ASN374 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GTP E 553 |
| Chain | Residue |
| E | HIS209 |
| E | GLY210 |
| E | LEU257 |
| E | ARG261 |
| E | TYR262 |
| E | ARG265 |
| E | GLU292 |
| E | LYS446 |
| site_id | BC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP F 551 |
| Chain | Residue |
| F | ARG94 |
| F | ASP168 |
| F | MET169 |
| F | SER170 |
| F | ARG211 |
| F | THR215 |
| F | GLN250 |
| F | PHE252 |
| F | GLY253 |
| F | ASN254 |
| F | VAL255 |
| F | GLU275 |
| F | SER276 |
| F | ALA326 |
| F | GLY347 |
| F | ALA348 |
| F | ASN349 |
| F | ASN374 |
| F | GLU550 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GTP F 553 |
| Chain | Residue |
| F | ILE212 |
| F | SER213 |
| F | ARG217 |
| F | HIS258 |
| F | ARG261 |
| F | TYR262 |
| F | ARG265 |
| F | LYS289 |
| F | GLU292 |
| F | HIS450 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE B1T E 552 |
| Chain | Residue |
| A | ARG146 |
| A | ARG147 |
| A | B1T552 |
| E | GLU142 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE B1T B 552 |
| Chain | Residue |
| B | ARG147 |
| B | MET150 |
| C | GLU142 |
| C | ARG146 |
| C | B1T552 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE B1T C 552 |
| Chain | Residue |
| B | ARG146 |
| B | THR186 |
| B | B1T552 |
| C | ARG146 |
| C | MET150 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE B1T D 552 |
| Chain | Residue |
| A | VAL498 |
| D | ARG146 |
| D | MET150 |
| F | B1T552 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE B1T A 552 |
| Chain | Residue |
| A | GLU142 |
| A | ARG146 |
| A | ASP181 |
| A | SER185 |
| E | ARG146 |
| E | ARG147 |
| E | B1T552 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE B1T F 552 |
| Chain | Residue |
| D | GLU142 |
| D | ARG146 |
| D | B1T552 |
| F | ARG146 |
| F | ARG147 |
| F | MET150 |
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 | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10011 |
| Chain | Residue | Details |
| A | GLY123 | |
| B | GLY123 | |
| C | GLY123 | |
| D | GLY123 | |
| E | GLY123 | |
| F | GLY123 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 66 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11254391 |
| Chain | Residue | Details |
| A | GLN81 | |
| A | VAL378 | |
| A | GLU384 | |
| B | GLN81 | |
| B | THR87 | |
| B | MET111 | |
| B | ALA116 | |
| B | ILE192 | |
| B | GLY206 | |
| B | GLY210 | |
| B | SER259 | |
| A | THR87 | |
| B | TYR262 | |
| B | VAL378 | |
| B | GLU384 | |
| C | GLN81 | |
| C | THR87 | |
| C | MET111 | |
| C | ALA116 | |
| C | ILE192 | |
| C | GLY206 | |
| C | GLY210 | |
| A | MET111 | |
| C | SER259 | |
| C | TYR262 | |
| C | VAL378 | |
| C | GLU384 | |
| D | GLN81 | |
| D | THR87 | |
| D | MET111 | |
| D | ALA116 | |
| D | ILE192 | |
| D | GLY206 | |
| A | ALA116 | |
| D | GLY210 | |
| D | SER259 | |
| D | TYR262 | |
| D | VAL378 | |
| D | GLU384 | |
| E | GLN81 | |
| E | THR87 | |
| E | MET111 | |
| E | ALA116 | |
| E | ILE192 | |
| A | ILE192 | |
| E | GLY206 | |
| E | GLY210 | |
| E | SER259 | |
| E | TYR262 | |
| E | VAL378 | |
| E | GLU384 | |
| F | GLN81 | |
| F | THR87 | |
| F | MET111 | |
| F | ALA116 | |
| A | GLY206 | |
| F | ILE192 | |
| F | GLY206 | |
| F | GLY210 | |
| F | SER259 | |
| F | TYR262 | |
| F | VAL378 | |
| F | GLU384 | |
| A | GLY210 | |
| A | SER259 | |
| A | TYR262 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12653548 |
| Chain | Residue | Details |
| A | ASN390 | |
| E | THR456 | |
| F | ASN390 | |
| F | THR456 | |
| A | THR456 | |
| B | ASN390 | |
| B | THR456 | |
| C | ASN390 | |
| C | THR456 | |
| D | ASN390 | |
| D | THR456 | |
| E | ASN390 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | ASN8 | |
| E | GLU140 | |
| F | ASN8 | |
| F | GLU140 | |
| A | GLU140 | |
| B | ASN8 | |
| B | GLU140 | |
| C | ASN8 | |
| C | GLU140 | |
| D | ASN8 | |
| D | GLU140 | |
| E | ASN8 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | ARG19 | |
| E | ASP68 | |
| F | ARG19 | |
| F | ASP68 | |
| A | ASP68 | |
| B | ARG19 | |
| B | ASP68 | |
| C | ARG19 | |
| C | ASP68 | |
| D | ARG19 | |
| D | ASP68 | |
| E | ARG19 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 54 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22076378 |
| Chain | Residue | Details |
| A | VAL24 | |
| B | VAL24 | |
| B | ARG50 | |
| B | ASP102 | |
| B | GLY303 | |
| B | GLU355 | |
| B | LEU397 | |
| B | ALA443 | |
| B | THR467 | |
| B | ALA485 | |
| C | VAL24 | |
| A | ARG50 | |
| C | ARG50 | |
| C | ASP102 | |
| C | GLY303 | |
| C | GLU355 | |
| C | LEU397 | |
| C | ALA443 | |
| C | THR467 | |
| C | ALA485 | |
| D | VAL24 | |
| D | ARG50 | |
| A | ASP102 | |
| D | ASP102 | |
| D | GLY303 | |
| D | GLU355 | |
| D | LEU397 | |
| D | ALA443 | |
| D | THR467 | |
| D | ALA485 | |
| E | VAL24 | |
| E | ARG50 | |
| E | ASP102 | |
| A | GLY303 | |
| E | GLY303 | |
| E | GLU355 | |
| E | LEU397 | |
| E | ALA443 | |
| E | THR467 | |
| E | ALA485 | |
| F | VAL24 | |
| F | ARG50 | |
| F | ASP102 | |
| F | GLY303 | |
| A | GLU355 | |
| F | GLU355 | |
| F | LEU397 | |
| F | ALA443 | |
| F | THR467 | |
| F | ALA485 | |
| A | LEU397 | |
| A | ALA443 | |
| A | THR467 | |
| A | ALA485 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 18 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22076378 |
| Chain | Residue | Details |
| A | GLU30 | |
| D | GLU30 | |
| D | ALA326 | |
| D | VAL339 | |
| E | GLU30 | |
| E | ALA326 | |
| E | VAL339 | |
| F | GLU30 | |
| F | ALA326 | |
| F | VAL339 | |
| A | ALA326 | |
| A | VAL339 | |
| B | GLU30 | |
| B | ALA326 | |
| B | VAL339 | |
| C | GLU30 | |
| C | ALA326 | |
| C | VAL339 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | ILE75 | |
| B | ILE75 | |
| C | ILE75 | |
| D | ILE75 | |
| E | ILE75 | |
| F | ILE75 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | THR87 | |
| B | THR87 | |
| C | THR87 | |
| D | THR87 | |
| E | THR87 | |
| F | THR87 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | MET111 | |
| C | ALA127 | |
| C | GLU151 | |
| C | PHE266 | |
| D | MET111 | |
| D | ALA127 | |
| D | GLU151 | |
| D | PHE266 | |
| E | MET111 | |
| E | ALA127 | |
| E | GLU151 | |
| A | ALA127 | |
| E | PHE266 | |
| F | MET111 | |
| F | ALA127 | |
| F | GLU151 | |
| F | PHE266 | |
| A | GLU151 | |
| A | PHE266 | |
| B | MET111 | |
| B | ALA127 | |
| B | GLU151 | |
| B | PHE266 | |
| C | MET111 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 6 |
| Details | MOD_RES: ADP-ribosylcysteine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | THR112 | |
| B | THR112 | |
| C | THR112 | |
| D | THR112 | |
| E | THR112 | |
| F | THR112 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 48 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26443 |
| Chain | Residue | Details |
| A | GLY123 | |
| B | ILE131 | |
| B | ILE286 | |
| B | GLU292 | |
| B | PRO305 | |
| B | GLN330 | |
| B | LEU417 | |
| B | LYS420 | |
| C | GLY123 | |
| C | ILE131 | |
| C | ILE286 | |
| A | ILE131 | |
| C | GLU292 | |
| C | PRO305 | |
| C | GLN330 | |
| C | LEU417 | |
| C | LYS420 | |
| D | GLY123 | |
| D | ILE131 | |
| D | ILE286 | |
| D | GLU292 | |
| D | PRO305 | |
| A | ILE286 | |
| D | GLN330 | |
| D | LEU417 | |
| D | LYS420 | |
| E | GLY123 | |
| E | ILE131 | |
| E | ILE286 | |
| E | GLU292 | |
| E | PRO305 | |
| E | GLN330 | |
| E | LEU417 | |
| A | GLU292 | |
| E | LYS420 | |
| F | GLY123 | |
| F | ILE131 | |
| F | ILE286 | |
| F | GLU292 | |
| F | PRO305 | |
| F | GLN330 | |
| F | LEU417 | |
| F | LYS420 | |
| A | PRO305 | |
| A | GLN330 | |
| A | LEU417 | |
| A | LYS420 | |
| B | GLY123 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | PRO167 | |
| E | PRO324 | |
| F | PRO167 | |
| F | PRO324 | |
| A | PRO324 | |
| B | PRO167 | |
| B | PRO324 | |
| C | PRO167 | |
| C | PRO324 | |
| D | PRO167 | |
| D | PRO324 | |
| E | PRO167 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10860 |
| Chain | Residue | Details |
| A | GLY350 | |
| B | GLY350 | |
| C | GLY350 | |
| D | GLY350 | |
| E | GLY350 | |
| F | GLY350 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00367 |
| Chain | Residue | Details |
| A | GLY452 | |
| B | GLY452 | |
| C | GLY452 | |
| D | GLY452 | |
| E | GLY452 | |
| F | GLY452 |
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 | 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 |
