7VDA
2.26 A structure of the glutamate dehydrogenase
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 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 | LYS126 | |
B | LYS126 | |
C | LYS126 | |
D | LYS126 | |
E | LYS126 | |
F | LYS126 |
site_id | SWS_FT_FI2 |
Number of Residues | 66 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11254391 |
Chain | Residue | Details |
A | GLN84 | |
A | SER381 | |
A | LYS387 | |
B | GLN84 | |
B | LYS90 | |
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 | |
A | SER213 | |
A | TYR262 | |
A | ARG265 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12653548 |
Chain | Residue | Details |
A | SER393 | |
E | ARG459 | |
F | SER393 | |
F | ARG459 | |
A | ARG459 | |
B | SER393 | |
B | ARG459 | |
C | SER393 | |
C | ARG459 | |
D | SER393 | |
D | ARG459 | |
E | SER393 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | LYS11 | |
E | LYS143 | |
F | LYS11 | |
F | LYS143 | |
A | LYS143 | |
B | LYS11 | |
B | LYS143 | |
C | LYS11 | |
C | LYS143 | |
D | LYS11 | |
D | LYS143 | |
E | LYS11 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | SER22 | |
E | SER71 | |
F | SER22 | |
F | SER71 | |
A | SER71 | |
B | SER22 | |
B | SER71 | |
C | SER22 | |
C | SER71 | |
D | SER22 | |
D | SER71 | |
E | SER22 |
site_id | SWS_FT_FI6 |
Number of Residues | 54 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22076378 |
Chain | Residue | Details |
A | LYS27 | |
B | LYS27 | |
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 | |
A | LYS400 | |
A | LYS446 | |
A | LYS470 | |
A | LYS488 |
site_id | SWS_FT_FI7 |
Number of Residues | 18 |
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 | |
A | LYS329 | |
A | LYS342 | |
B | LYS33 | |
B | LYS329 | |
B | LYS342 | |
C | LYS33 | |
C | LYS329 | |
C | LYS342 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P26443 |
Chain | Residue | Details |
A | TYR78 | |
B | TYR78 | |
C | TYR78 | |
D | TYR78 | |
E | TYR78 | |
F | TYR78 |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00367 |
Chain | Residue | Details |
A | LYS90 | |
B | LYS90 | |
C | LYS90 | |
D | LYS90 | |
E | LYS90 | |
F | LYS90 |
site_id | SWS_FT_FI10 |
Number of Residues | 24 |
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 | |
A | LYS154 | |
A | LYS269 | |
B | LYS114 | |
B | LYS130 | |
B | LYS154 | |
B | LYS269 | |
C | LYS114 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | MOD_RES: ADP-ribosylcysteine => ECO:0000250|UniProtKB:P00367 |
Chain | Residue | Details |
A | CYS115 | |
B | CYS115 | |
C | CYS115 | |
D | CYS115 | |
E | CYS115 | |
F | CYS115 |
site_id | SWS_FT_FI12 |
Number of Residues | 48 |
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 | |
A | LYS308 | |
A | LYS333 | |
A | LYS420 | |
A | LYS423 | |
B | LYS126 |
site_id | SWS_FT_FI13 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00367 |
Chain | Residue | Details |
A | SER170 | |
E | SER327 | |
F | SER170 | |
F | SER327 | |
A | SER327 | |
B | SER170 | |
B | SER327 | |
C | SER170 | |
C | SER327 | |
D | SER170 | |
D | SER327 | |
E | SER170 |
site_id | SWS_FT_FI14 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10860 |
Chain | Residue | Details |
A | THR353 | |
B | THR353 | |
C | THR353 | |
D | THR353 | |
E | THR353 | |
F | THR353 |
site_id | SWS_FT_FI15 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00367 |
Chain | Residue | Details |
A | TYR455 | |
B | TYR455 | |
C | TYR455 | |
D | TYR455 | |
E | TYR455 | |
F | TYR455 |