1HWY
BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NAD AND 2-OXOGLUTARATE
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 | 7 |
Details | BINDING SITE FOR RESIDUE PO4 E 502 |
Chain | Residue |
E | SER213 |
E | ARG261 |
E | TYR262 |
E | PO4503 |
E | PO4505 |
E | HOH511 |
E | HOH512 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 D 502 |
Chain | Residue |
D | TYR262 |
D | PO4503 |
D | PO4505 |
D | HOH509 |
D | HOH510 |
D | SER213 |
D | ARG261 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 C 502 |
Chain | Residue |
C | SER213 |
C | ARG261 |
C | TYR262 |
C | PO4503 |
C | PO4504 |
C | HOH509 |
C | HOH510 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 502 |
Chain | Residue |
B | SER213 |
B | ARG261 |
B | TYR262 |
B | PO4503 |
B | PO4504 |
B | HOH511 |
B | HOH512 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 F 502 |
Chain | Residue |
F | ARG217 |
F | HIS450 |
F | HOH510 |
F | HOH513 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 F 503 |
Chain | Residue |
F | SER213 |
F | ARG261 |
F | TYR262 |
F | PO4504 |
F | PO4505 |
F | HOH511 |
F | HOH512 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 F 504 |
Chain | Residue |
F | HIS209 |
F | GLY210 |
F | PO4503 |
F | PO4505 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 E 503 |
Chain | Residue |
E | HIS209 |
E | GLY210 |
E | PO4502 |
E | PO4505 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 D 503 |
Chain | Residue |
D | HIS209 |
D | GLY210 |
D | PO4502 |
D | PO4505 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 503 |
Chain | Residue |
C | HIS209 |
C | GLY210 |
C | PO4502 |
C | PO4504 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 503 |
Chain | Residue |
B | HIS209 |
B | GLY210 |
B | PO4502 |
B | PO4504 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 E 504 |
Chain | Residue |
E | ARG217 |
E | HIS450 |
E | HOH510 |
E | HOH513 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 504 |
Chain | Residue |
B | PO4502 |
B | PO4503 |
B | HOH510 |
B | HOH512 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 502 |
Chain | Residue |
A | HIS209 |
A | GLY210 |
A | PO4503 |
A | PO4505 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 503 |
Chain | Residue |
A | SER213 |
A | ARG261 |
A | TYR262 |
A | PO4502 |
A | PO4505 |
A | HOH509 |
A | HOH510 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 504 |
Chain | Residue |
A | ARG217 |
A | HIS450 |
A | HOH511 |
A | HOH514 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 505 |
Chain | Residue |
A | PO4502 |
A | PO4503 |
A | HOH510 |
A | HOH514 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 504 |
Chain | Residue |
C | PO4502 |
C | PO4503 |
C | HOH510 |
C | HOH514 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 D 504 |
Chain | Residue |
D | ARG217 |
D | HIS450 |
D | HOH511 |
D | HOH514 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 505 |
Chain | Residue |
C | ARG217 |
C | HIS450 |
C | HOH511 |
C | HOH514 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 505 |
Chain | Residue |
B | HIS450 |
B | HOH510 |
B | HOH513 |
B | ARG217 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 F 505 |
Chain | Residue |
F | PO4503 |
F | PO4504 |
F | HOH510 |
F | HOH512 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 E 505 |
Chain | Residue |
E | PO4502 |
E | PO4503 |
E | HOH510 |
E | HOH512 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 D 505 |
Chain | Residue |
D | PO4502 |
D | PO4503 |
D | HOH510 |
D | HOH514 |
site_id | CC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AKG F 506 |
Chain | Residue |
F | LYS90 |
F | GLY92 |
F | MET111 |
F | LYS114 |
F | LYS126 |
F | ALA166 |
F | PRO167 |
F | ASN168 |
F | THR199 |
F | ARG211 |
F | ASN349 |
F | ASN374 |
F | VAL378 |
F | SER381 |
F | NAD507 |
site_id | CC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AKG D 506 |
Chain | Residue |
D | LYS90 |
D | GLY92 |
D | MET111 |
D | LYS114 |
D | LYS126 |
D | ALA166 |
D | PRO167 |
D | ASN168 |
D | THR199 |
D | ARG211 |
D | ASN349 |
D | ASN374 |
D | VAL378 |
D | SER381 |
D | NAD508 |
site_id | CC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AKG C 506 |
Chain | Residue |
C | LYS90 |
C | GLY92 |
C | MET111 |
C | LYS114 |
C | LYS126 |
C | ALA166 |
C | PRO167 |
C | ASN168 |
C | THR199 |
C | ARG211 |
C | ASN349 |
C | ASN374 |
C | VAL378 |
C | SER381 |
C | NAD508 |
site_id | DC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AKG E 506 |
Chain | Residue |
E | LYS90 |
E | GLY92 |
E | MET111 |
E | LYS114 |
E | LYS126 |
E | ALA166 |
E | PRO167 |
E | ASN168 |
E | THR199 |
E | ARG211 |
E | ASN349 |
E | ASN374 |
E | VAL378 |
E | SER381 |
E | NAD508 |
site_id | DC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AKG B 506 |
Chain | Residue |
B | LYS90 |
B | GLY92 |
B | MET111 |
B | LYS114 |
B | LYS126 |
B | ALA166 |
B | PRO167 |
B | ASN168 |
B | THR199 |
B | ARG211 |
B | ASN349 |
B | ASN374 |
B | VAL378 |
B | SER381 |
B | NAD508 |
site_id | DC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AKG A 506 |
Chain | Residue |
A | LYS90 |
A | GLY92 |
A | MET111 |
A | LYS114 |
A | LYS126 |
A | ALA166 |
A | PRO167 |
A | ASN168 |
A | THR199 |
A | ARG211 |
A | ASN349 |
A | ASN374 |
A | VAL378 |
A | SER381 |
A | NAD508 |
site_id | DC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD D 507 |
Chain | Residue |
C | GLN85 |
C | ARG86 |
C | THR87 |
C | CYS115 |
C | ALA116 |
C | ASP119 |
C | VAL120 |
C | PRO121 |
C | ARG459 |
C | LYS488 |
C | VAL489 |
D | HIS195 |
D | GLN205 |
D | GLY206 |
D | LYS387 |
D | ASN388 |
D | ASN390 |
D | HIS391 |
D | VAL392 |
D | SER393 |
D | ARG396 |
D | GLU445 |
site_id | DC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD A 507 |
Chain | Residue |
A | HIS195 |
A | GLN205 |
A | GLY206 |
A | LYS387 |
A | ASN388 |
A | ASN390 |
A | HIS391 |
A | VAL392 |
A | SER393 |
A | ARG396 |
B | GLN85 |
B | ARG86 |
B | THR87 |
B | CYS115 |
B | ALA116 |
B | ASP119 |
B | VAL120 |
B | PRO121 |
B | ARG459 |
B | LYS488 |
B | VAL489 |
site_id | DC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD F 507 |
Chain | Residue |
F | ARG94 |
F | ASN168 |
F | MET169 |
F | SER170 |
F | ARG211 |
F | THR215 |
F | GLY251 |
F | PHE252 |
F | GLY253 |
F | ASN254 |
F | VAL255 |
F | GLU275 |
F | SER276 |
F | LYS295 |
F | ALA325 |
F | ALA326 |
F | SER327 |
F | GLN330 |
F | GLY347 |
F | ALA348 |
F | ASN349 |
F | ASN374 |
F | AKG506 |
site_id | DC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD E 507 |
Chain | Residue |
D | GLN85 |
D | ARG86 |
D | THR87 |
D | CYS115 |
D | ALA116 |
D | ASP119 |
D | VAL120 |
D | PRO121 |
D | ARG459 |
D | LYS488 |
D | VAL489 |
E | HIS195 |
E | GLY206 |
E | LYS387 |
E | ASN388 |
E | ASN390 |
E | HIS391 |
E | VAL392 |
E | SER393 |
E | ARG396 |
E | GLU445 |
site_id | DC8 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD B 507 |
Chain | Residue |
B | HIS195 |
B | GLN205 |
B | GLY206 |
B | LYS387 |
B | ASN388 |
B | ASN390 |
B | HIS391 |
B | VAL392 |
B | SER393 |
B | ARG396 |
B | GLU445 |
F | GLN85 |
F | ARG86 |
F | THR87 |
F | CYS115 |
F | ALA116 |
F | ASP119 |
F | VAL120 |
F | PRO121 |
F | ARG459 |
F | LYS488 |
F | VAL489 |
site_id | DC9 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD C 507 |
Chain | Residue |
C | HIS195 |
C | GLN205 |
C | GLY206 |
C | LYS387 |
C | ASN388 |
C | ASN390 |
C | HIS391 |
C | VAL392 |
C | SER393 |
C | ARG396 |
C | GLU445 |
E | GLN85 |
E | ARG86 |
E | THR87 |
E | CYS115 |
E | ALA116 |
E | ASP119 |
E | VAL120 |
E | PRO121 |
E | ARG459 |
E | LYS488 |
E | VAL489 |
site_id | EC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD C 508 |
Chain | Residue |
C | ARG94 |
C | ASN168 |
C | MET169 |
C | SER170 |
C | ARG211 |
C | THR215 |
C | GLY251 |
C | PHE252 |
C | GLY253 |
C | ASN254 |
C | VAL255 |
C | GLU275 |
C | SER276 |
C | LYS295 |
C | ALA325 |
C | ALA326 |
C | SER327 |
C | GLN330 |
C | GLY347 |
C | ALA348 |
C | ASN349 |
C | ASN374 |
C | AKG506 |
site_id | EC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD A 508 |
Chain | Residue |
A | ARG94 |
A | ASN168 |
A | MET169 |
A | SER170 |
A | ARG211 |
A | THR215 |
A | GLY251 |
A | PHE252 |
A | GLY253 |
A | ASN254 |
A | VAL255 |
A | GLU275 |
A | SER276 |
A | LYS295 |
A | ALA325 |
A | ALA326 |
A | SER327 |
A | GLN330 |
A | GLY347 |
A | ALA348 |
A | ASN349 |
A | ASN374 |
A | AKG506 |
site_id | EC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD F 508 |
Chain | Residue |
A | GLN85 |
A | ARG86 |
A | THR87 |
A | CYS115 |
A | ALA116 |
A | ASP119 |
A | VAL120 |
A | PRO121 |
A | ARG459 |
A | LYS488 |
A | VAL489 |
F | HIS195 |
F | GLN205 |
F | GLY206 |
F | LYS387 |
F | ASN388 |
F | ASN390 |
F | HIS391 |
F | VAL392 |
F | SER393 |
F | ARG396 |
F | GLU445 |
site_id | EC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD B 508 |
Chain | Residue |
B | ARG94 |
B | ASN168 |
B | MET169 |
B | SER170 |
B | ARG211 |
B | THR215 |
B | GLY251 |
B | PHE252 |
B | GLY253 |
B | ASN254 |
B | VAL255 |
B | GLU275 |
B | SER276 |
B | LYS295 |
B | ALA325 |
B | ALA326 |
B | SER327 |
B | GLN330 |
B | GLY347 |
B | ALA348 |
B | ASN349 |
B | ASN374 |
B | AKG506 |
site_id | EC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD D 508 |
Chain | Residue |
D | ARG94 |
D | ASN168 |
D | MET169 |
D | SER170 |
D | ARG211 |
D | THR215 |
D | GLY251 |
D | PHE252 |
D | GLY253 |
D | ASN254 |
D | VAL255 |
D | GLU275 |
D | SER276 |
D | LYS295 |
D | ALA325 |
D | ALA326 |
D | SER327 |
D | GLN330 |
D | GLY347 |
D | ALA348 |
D | ASN349 |
D | ASN374 |
D | AKG506 |
site_id | EC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD E 508 |
Chain | Residue |
E | ARG94 |
E | ASN168 |
E | MET169 |
E | SER170 |
E | ARG211 |
E | THR215 |
E | GLY251 |
E | PHE252 |
E | GLY253 |
E | ASN254 |
E | VAL255 |
E | GLU275 |
E | SER276 |
E | LYS295 |
E | ALA325 |
E | ALA326 |
E | SER327 |
E | GLN330 |
E | GLY347 |
E | ALA348 |
E | ASN349 |
E | ASN374 |
E | AKG506 |
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 | TYR183 | |
B | TYR183 | |
C | TYR183 | |
D | TYR183 | |
E | TYR183 | |
F | TYR183 |
site_id | SWS_FT_FI2 |
Number of Residues | 66 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11254391 |
Chain | Residue | Details |
A | LEU141 | |
A | ASP438 | |
A | SER444 | |
B | LEU141 | |
B | ARG147 | |
B | THR171 | |
B | MET176 | |
B | PHE252 | |
B | PHE266 | |
B | CYS270 | |
B | CYS319 | |
A | ARG147 | |
B | LEU322 | |
B | ASP438 | |
B | SER444 | |
C | LEU141 | |
C | ARG147 | |
C | THR171 | |
C | MET176 | |
C | PHE252 | |
C | PHE266 | |
C | CYS270 | |
A | THR171 | |
C | CYS319 | |
C | LEU322 | |
C | ASP438 | |
C | SER444 | |
D | LEU141 | |
D | ARG147 | |
D | THR171 | |
D | MET176 | |
D | PHE252 | |
D | PHE266 | |
A | MET176 | |
D | CYS270 | |
D | CYS319 | |
D | LEU322 | |
D | ASP438 | |
D | SER444 | |
E | LEU141 | |
E | ARG147 | |
E | THR171 | |
E | MET176 | |
E | PHE252 | |
A | PHE252 | |
E | PHE266 | |
E | CYS270 | |
E | CYS319 | |
E | LEU322 | |
E | ASP438 | |
E | SER444 | |
F | LEU141 | |
F | ARG147 | |
F | THR171 | |
F | MET176 | |
A | PHE266 | |
F | PHE252 | |
F | PHE266 | |
F | CYS270 | |
F | CYS319 | |
F | LEU322 | |
F | ASP438 | |
F | SER444 | |
A | CYS270 | |
A | CYS319 | |
A | LEU322 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12653548 |
Chain | Residue | Details |
A | HIS450 | |
B | HIS450 | |
C | HIS450 | |
D | HIS450 | |
E | HIS450 | |
F | HIS450 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | ASP68 | |
E | GLY200 | |
F | ASP68 | |
F | GLY200 | |
A | GLY200 | |
B | ASP68 | |
B | GLY200 | |
C | ASP68 | |
C | GLY200 | |
D | ASP68 | |
D | GLY200 | |
E | ASP68 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | ARG79 | |
E | GLY128 | |
F | ARG79 | |
F | GLY128 | |
A | GLY128 | |
B | ARG79 | |
B | GLY128 | |
C | ARG79 | |
C | GLY128 | |
D | ARG79 | |
D | GLY128 | |
E | ARG79 |
site_id | SWS_FT_FI6 |
Number of Residues | 36 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22076378 |
Chain | Residue | Details |
A | HIS84 | |
B | ARG363 | |
B | GLU415 | |
B | MET457 | |
C | HIS84 | |
C | LEU110 | |
C | VAL162 | |
C | ARG363 | |
C | GLU415 | |
C | MET457 | |
D | HIS84 | |
A | LEU110 | |
D | LEU110 | |
D | VAL162 | |
D | ARG363 | |
D | GLU415 | |
D | MET457 | |
E | HIS84 | |
E | LEU110 | |
E | VAL162 | |
E | ARG363 | |
E | GLU415 | |
A | VAL162 | |
E | MET457 | |
F | HIS84 | |
F | LEU110 | |
F | VAL162 | |
F | ARG363 | |
F | GLU415 | |
F | MET457 | |
A | ARG363 | |
A | GLU415 | |
A | MET457 | |
B | HIS84 | |
B | LEU110 | |
B | VAL162 |
site_id | SWS_FT_FI7 |
Number of Residues | 18 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22076378 |
Chain | Residue | Details |
A | LYS90 | |
D | LYS90 | |
D | LEU386 | |
D | PHE399 | |
E | LYS90 | |
E | LEU386 | |
E | PHE399 | |
F | LYS90 | |
F | LEU386 | |
F | PHE399 | |
A | LEU386 | |
A | PHE399 | |
B | LYS90 | |
B | LEU386 | |
B | PHE399 | |
C | LYS90 | |
C | LEU386 | |
C | PHE399 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | ASN135 | |
B | ASN135 | |
C | ASN135 | |
D | ASN135 | |
E | ASN135 | |
F | ASN135 |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00367 |
Chain | Residue | Details |
A | ARG147 | |
B | ARG147 | |
C | ARG147 | |
D | ARG147 | |
E | ARG147 | |
F | ARG147 |
site_id | SWS_FT_FI10 |
Number of Residues | 24 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | THR171 | |
C | ILE187 | |
C | ARG211 | |
C | ALA326 | |
D | THR171 | |
D | ILE187 | |
D | ARG211 | |
D | ALA326 | |
E | THR171 | |
E | ILE187 | |
E | ARG211 | |
A | ILE187 | |
E | ALA326 | |
F | THR171 | |
F | ILE187 | |
F | ARG211 | |
F | ALA326 | |
A | ARG211 | |
A | ALA326 | |
B | THR171 | |
B | ILE187 | |
B | ARG211 | |
B | ALA326 | |
C | THR171 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | MOD_RES: ADP-ribosylcysteine => ECO:0000250|UniProtKB:P00367 |
Chain | Residue | Details |
A | GLY172 | |
B | GLY172 | |
C | GLY172 | |
D | GLY172 | |
E | GLY172 | |
F | GLY172 |
site_id | SWS_FT_FI12 |
Number of Residues | 48 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | TYR183 | |
B | ASP191 | |
B | GLU346 | |
B | THR352 | |
B | ILE365 | |
B | ASN390 | |
B | LEU477 | |
B | ALA480 | |
C | TYR183 | |
C | ASP191 | |
C | GLU346 | |
A | ASP191 | |
C | THR352 | |
C | ILE365 | |
C | ASN390 | |
C | LEU477 | |
C | ALA480 | |
D | TYR183 | |
D | ASP191 | |
D | GLU346 | |
D | THR352 | |
D | ILE365 | |
A | GLU346 | |
D | ASN390 | |
D | LEU477 | |
D | ALA480 | |
E | TYR183 | |
E | ASP191 | |
E | GLU346 | |
E | THR352 | |
E | ILE365 | |
E | ASN390 | |
E | LEU477 | |
A | THR352 | |
E | ALA480 | |
F | TYR183 | |
F | ASP191 | |
F | GLU346 | |
F | THR352 | |
F | ILE365 | |
F | ASN390 | |
F | LEU477 | |
F | ALA480 | |
A | ILE365 | |
A | ASN390 | |
A | LEU477 | |
A | ALA480 | |
B | TYR183 |
site_id | SWS_FT_FI13 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00367 |
Chain | Residue | Details |
A | ILE227 | |
E | GLN384 | |
F | ILE227 | |
F | GLN384 | |
A | GLN384 | |
B | ILE227 | |
B | GLN384 | |
C | ILE227 | |
C | GLN384 | |
D | ILE227 | |
D | GLN384 | |
E | ILE227 |
site_id | SWS_FT_FI14 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10860 |
Chain | Residue | Details |
A | LEU410 | |
B | LEU410 | |
C | LEU410 | |
D | LEU410 | |
E | LEU410 | |
F | LEU410 |
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 | ASN168 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
B | LYS126 | |
B | ASN168 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
C | LYS126 | |
C | ASN168 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
D | LYS126 | |
D | ASN168 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
E | LYS126 | |
E | ASN168 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hrd |
Chain | Residue | Details |
F | LYS126 | |
F | ASN168 |