3ETE
Crystal structure of bovine glutamate dehydrogenase complexed with hexachlorophene
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 | ASN254 |
A | VAL255 |
A | GLU275 |
A | SER276 |
A | ALA326 |
A | SER327 |
A | GLN330 |
A | ALA348 |
A | ASN349 |
A | ASN374 |
A | LYS134 |
A | GLU550 |
A | ASP168 |
A | MET169 |
A | SER170 |
A | ARG211 |
A | THR215 |
A | PHE252 |
A | GLY253 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GTP A 553 |
Chain | Residue |
A | ILE212 |
A | SER213 |
A | ARG217 |
A | LEU257 |
A | HIS258 |
A | ARG261 |
A | TYR262 |
A | GLU292 |
A | LYS446 |
A | HIS450 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NDP B 551 |
Chain | Residue |
B | ARG94 |
B | LYS134 |
B | PRO167 |
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 | SER327 |
B | GLN330 |
B | GLY347 |
B | ALA348 |
B | ASN349 |
B | ASN374 |
B | GLU550 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GTP B 553 |
Chain | Residue |
B | HIS209 |
B | ARG217 |
B | HIS258 |
B | ARG261 |
B | TYR262 |
B | ARG265 |
B | GLU292 |
B | HIS450 |
B | HOH554 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NDP C 551 |
Chain | Residue |
C | ARG94 |
C | LYS134 |
C | PRO167 |
C | ASP168 |
C | MET169 |
C | SER170 |
C | ARG211 |
C | THR215 |
C | PHE252 |
C | GLY253 |
C | ASN254 |
C | VAL255 |
C | GLU275 |
C | SER276 |
C | ALA325 |
C | ALA326 |
C | GLN330 |
C | GLY347 |
C | ASN349 |
C | ASN374 |
C | GLU550 |
C | HOH582 |
C | HOH590 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GTP C 553 |
Chain | Residue |
C | HIS209 |
C | ARG217 |
C | HIS258 |
C | ARG261 |
C | TYR262 |
C | ARG265 |
C | LYS289 |
C | GLU292 |
site_id | AC7 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NDP D 551 |
Chain | Residue |
D | THR215 |
D | GLY251 |
D | PHE252 |
D | GLY253 |
D | ASN254 |
D | VAL255 |
D | GLU275 |
D | SER276 |
D | ALA325 |
D | ALA326 |
D | SER327 |
D | GLN330 |
D | GLY347 |
D | ALA348 |
D | ASN349 |
D | ASN374 |
D | GLU550 |
D | HOH560 |
D | ARG94 |
D | LYS134 |
D | ASP168 |
D | MET169 |
D | SER170 |
D | ARG211 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GTP D 553 |
Chain | Residue |
D | HIS209 |
D | ARG217 |
D | HIS258 |
D | ARG261 |
D | TYR262 |
D | ARG265 |
D | GLU292 |
D | HIS450 |
D | HOH554 |
D | HOH567 |
D | HOH573 |
D | HOH586 |
site_id | AC9 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NDP E 551 |
Chain | Residue |
E | ARG94 |
E | LYS134 |
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 | ALA325 |
E | ALA326 |
E | SER327 |
E | GLN330 |
E | ALA348 |
E | ASN349 |
E | GLU550 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GTP E 553 |
Chain | Residue |
E | HIS209 |
E | ARG217 |
E | LEU257 |
E | HIS258 |
E | ARG261 |
E | TYR262 |
E | ARG265 |
E | GLU292 |
E | HIS450 |
E | HOH572 |
site_id | BC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NDP F 551 |
Chain | Residue |
F | ARG94 |
F | LYS134 |
F | ASP168 |
F | MET169 |
F | ARG211 |
F | THR215 |
F | PHE252 |
F | GLY253 |
F | ASN254 |
F | VAL255 |
F | GLU275 |
F | SER276 |
F | ALA326 |
F | SER327 |
F | GLN330 |
F | GLY347 |
F | ALA348 |
F | ASN349 |
F | ASN374 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GTP F 553 |
Chain | Residue |
F | HIS209 |
F | ARG217 |
F | HIS258 |
F | ARG261 |
F | TYR262 |
F | ARG265 |
F | GLU292 |
F | HIS450 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE H3P B 552 |
Chain | Residue |
A | TYR190 |
A | H3P552 |
B | ALA153 |
B | ILE158 |
B | TYR183 |
E | LYS154 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE H3P A 552 |
Chain | Residue |
A | THR186 |
A | ILE187 |
A | TYR190 |
A | HOH560 |
B | H3P552 |
E | MET150 |
E | THR186 |
E | ILE187 |
E | HIS189 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE H3P D 552 |
Chain | Residue |
A | ALA153 |
D | ALA153 |
D | LYS154 |
E | TYR190 |
F | H3P552 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE H3P F 552 |
Chain | Residue |
D | MET150 |
D | THR186 |
D | ILE187 |
D | HIS189 |
D | H3P552 |
F | LYS154 |
F | THR186 |
F | ILE187 |
F | TYR190 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE H3P C 552 |
Chain | Residue |
C | ALA153 |
C | LYS154 |
C | H3P554 |
D | TYR190 |
F | ALA153 |
F | LYS154 |
F | HOH572 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE H3P C 554 |
Chain | Residue |
B | THR186 |
B | ILE187 |
B | TYR190 |
C | MET150 |
C | THR186 |
C | ILE187 |
C | HIS189 |
C | H3P552 |
C | HOH574 |
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 |