3AOG
Crystal structure of glutamate dehydrogenase (GdhB) from Thermus thermophilus (Glu bound form)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
A | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
B | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
B | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
C | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
C | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
D | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
D | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
D | 0006520 | biological_process | amino acid metabolic process |
D | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
E | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
E | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
E | 0006520 | biological_process | amino acid metabolic process |
E | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
F | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
F | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
F | 0006520 | biological_process | amino acid metabolic process |
F | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
G | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
G | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
G | 0006520 | biological_process | amino acid metabolic process |
G | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
H | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
H | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
H | 0006520 | biological_process | amino acid metabolic process |
H | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
I | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
I | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
I | 0006520 | biological_process | amino acid metabolic process |
I | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
J | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
J | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
J | 0006520 | biological_process | amino acid metabolic process |
J | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
K | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
K | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
K | 0006520 | biological_process | amino acid metabolic process |
K | 0006538 | biological_process | glutamate catabolic 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 | 0000166 | molecular_function | nucleotide binding |
L | 0004352 | molecular_function | glutamate dehydrogenase (NAD+) activity |
L | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
L | 0006520 | biological_process | amino acid metabolic process |
L | 0006538 | biological_process | glutamate catabolic 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 | 11 |
Details | BINDING SITE FOR RESIDUE GLU A 500 |
Chain | Residue |
A | GLY80 |
A | HOH671 |
A | HOH1052 |
A | MET99 |
A | LYS114 |
A | ALA152 |
A | PRO153 |
A | ASP154 |
A | ARG194 |
A | VAL354 |
A | SER357 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLU A 425 |
Chain | Residue |
A | ALA73 |
A | ARG417 |
A | ARG420 |
A | GLY421 |
A | LEU422 |
A | TYR423 |
A | HOH469 |
B | ARG135 |
E | ASP167 |
E | MET171 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLU B 500 |
Chain | Residue |
B | GLY80 |
B | MET99 |
B | LYS114 |
B | ALA152 |
B | PRO153 |
B | ASP154 |
B | ARG194 |
B | VAL354 |
B | SER357 |
B | HOH835 |
B | HOH1737 |
B | HOH1812 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLU B 425 |
Chain | Residue |
A | ARG135 |
B | THR72 |
B | ALA73 |
B | ARG420 |
B | GLY421 |
B | LEU422 |
B | TYR423 |
B | HOH440 |
B | HOH1358 |
D | ASP167 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLU C 500 |
Chain | Residue |
C | GLY80 |
C | MET99 |
C | LYS114 |
C | ALA152 |
C | PRO153 |
C | ASP154 |
C | SER357 |
C | HOH453 |
C | HOH746 |
C | HOH1253 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GLU C 425 |
Chain | Residue |
A | ASP167 |
A | MET171 |
C | ALA73 |
C | ARG417 |
C | ARG420 |
C | GLY421 |
C | LEU422 |
C | TYR423 |
C | HOH435 |
C | HOH1188 |
D | ARG135 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU D 500 |
Chain | Residue |
D | GLY80 |
D | MET99 |
D | LYS114 |
D | PRO153 |
D | ASP154 |
D | ARG194 |
D | SER357 |
D | HOH431 |
D | HOH1801 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU D 425 |
Chain | Residue |
C | ARG135 |
D | ALA73 |
D | ARG420 |
D | GLY421 |
D | LEU422 |
D | TYR423 |
D | HOH447 |
D | HOH591 |
F | ASP167 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU E 500 |
Chain | Residue |
E | GLY79 |
E | GLY80 |
E | MET99 |
E | LYS114 |
E | PRO153 |
E | ASP154 |
E | VAL354 |
E | SER357 |
E | HOH1522 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLU E 425 |
Chain | Residue |
E | HOH1363 |
F | ARG135 |
C | ASP167 |
C | MET171 |
E | ALA73 |
E | ARG420 |
E | GLY421 |
E | LEU422 |
E | TYR423 |
E | HOH846 |
site_id | BC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLU F 500 |
Chain | Residue |
F | GLY80 |
F | MET99 |
F | LYS114 |
F | ALA152 |
F | PRO153 |
F | ASP154 |
F | ARG194 |
F | VAL354 |
F | SER357 |
F | HOH979 |
F | HOH1542 |
F | HOH1798 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLU F 425 |
Chain | Residue |
B | ASP167 |
B | MET171 |
E | ARG135 |
F | ALA73 |
F | ARG417 |
F | ARG420 |
F | GLY421 |
F | LEU422 |
F | TYR423 |
F | HOH432 |
F | HOH445 |
F | HOH961 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU G 500 |
Chain | Residue |
G | GLY80 |
G | MET99 |
G | LYS114 |
G | ALA152 |
G | PRO153 |
G | ASP154 |
G | ARG194 |
G | SER357 |
G | HOH471 |
site_id | BC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GLU G 425 |
Chain | Residue |
G | ALA73 |
G | ARG417 |
G | ARG420 |
G | GLY421 |
G | LEU422 |
G | TYR423 |
G | HOH474 |
G | HOH881 |
I | ASP167 |
I | MET171 |
J | ARG135 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU H 500 |
Chain | Residue |
H | GLY80 |
H | MET99 |
H | LYS114 |
H | ALA152 |
H | PRO153 |
H | ASP154 |
H | ARG194 |
H | SER357 |
H | HOH1156 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU H 425 |
Chain | Residue |
G | ASP167 |
G | MET171 |
H | ARG417 |
H | ARG420 |
H | GLY421 |
H | LEU422 |
H | TYR423 |
H | HOH446 |
L | ARG135 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GLU I 500 |
Chain | Residue |
I | GLY80 |
I | MET99 |
I | LYS114 |
I | PRO153 |
I | ASP154 |
I | ARG194 |
I | SER357 |
I | HOH453 |
site_id | BC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLU I 425 |
Chain | Residue |
H | ASP167 |
I | THR72 |
I | ALA73 |
I | ARG420 |
I | GLY421 |
I | LEU422 |
I | TYR423 |
I | HOH451 |
I | HOH632 |
K | ARG135 |
site_id | CC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLU J 500 |
Chain | Residue |
J | GLY79 |
J | GLY80 |
J | MET99 |
J | LYS114 |
J | ALA152 |
J | PRO153 |
J | ASP154 |
J | VAL354 |
J | SER357 |
J | HOH1720 |
site_id | CC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLU J 425 |
Chain | Residue |
G | ARG135 |
J | LYS44 |
J | ALA73 |
J | ARG417 |
J | ARG420 |
J | GLY421 |
J | LEU422 |
J | TYR423 |
J | HOH1124 |
J | HOH1420 |
L | ASP167 |
L | MET171 |
site_id | CC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GLU K 500 |
Chain | Residue |
K | GLY80 |
K | MET99 |
K | LYS114 |
K | PRO153 |
K | ASP154 |
K | ARG194 |
K | GLY353 |
K | SER357 |
site_id | CC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GLU K 425 |
Chain | Residue |
I | ARG135 |
J | ASP167 |
K | ALA73 |
K | ARG417 |
K | ARG420 |
K | GLY421 |
K | LEU422 |
K | TYR423 |
K | HOH436 |
K | HOH446 |
K | HOH1310 |
site_id | CC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU L 500 |
Chain | Residue |
L | GLY80 |
L | MET99 |
L | LYS114 |
L | PRO153 |
L | ASP154 |
L | ARG194 |
L | GLY353 |
L | SER357 |
L | HOH433 |
site_id | CC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GLU L 425 |
Chain | Residue |
H | ARG135 |
K | ASP167 |
K | MET171 |
L | ALA73 |
L | ARG420 |
L | GLY421 |
L | LEU422 |
L | TYR423 |
L | HOH1112 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 426 |
Chain | Residue |
A | TYR368 |
A | GLU374 |
A | HOH1697 |
C | ARG378 |
C | ARG381 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NH4 A 427 |
Chain | Residue |
A | ARG381 |
A | HOH433 |
A | HOH1369 |
E | TYR368 |
E | GLU374 |
site_id | CC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NH4 B 426 |
Chain | Residue |
B | HOH434 |
B | HOH449 |
site_id | DC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 426 |
Chain | Residue |
C | TYR368 |
C | GLU374 |
E | ARG378 |
E | ARG381 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 D 426 |
Chain | Residue |
B | ARG378 |
B | ARG381 |
D | TYR368 |
D | GLU374 |
D | HOH941 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 F 426 |
Chain | Residue |
B | TYR368 |
B | GLU374 |
F | ARG378 |
F | ARG381 |
F | HOH1407 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NH4 F 427 |
Chain | Residue |
F | HIS241 |
F | GLU380 |
F | HOH493 |
site_id | DC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 G 426 |
Chain | Residue |
G | TYR368 |
G | GLU374 |
G | HOH427 |
G | HOH928 |
H | ARG378 |
H | ARG381 |
site_id | DC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NH4 H 426 |
Chain | Residue |
H | LYS114 |
H | ASP154 |
H | HOH441 |
site_id | DC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 I 426 |
Chain | Residue |
G | ARG378 |
G | ARG381 |
G | HOH1343 |
I | TYR368 |
I | GLU374 |
I | HOH449 |
I | HOH966 |
site_id | DC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 I 427 |
Chain | Residue |
H | TYR368 |
H | GLU374 |
I | ARG378 |
I | ARG381 |
site_id | DC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 J 426 |
Chain | Residue |
J | ARG378 |
J | ARG381 |
J | HOH653 |
L | TYR368 |
L | GLU374 |
site_id | EC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NH4 J 427 |
Chain | Residue |
J | HIS241 |
J | GLU380 |
J | HOH1221 |
site_id | EC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 K 426 |
Chain | Residue |
K | TYR368 |
K | GLU374 |
L | ARG378 |
L | ARG381 |
site_id | EC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NH4 L 426 |
Chain | Residue |
L | LEU192 |
L | GLY193 |
L | GLU372 |
L | HOH432 |
Functional Information from PROSITE/UniProt
site_id | PS00074 |
Number of Residues | 14 |
Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGirvDP |
Chain | Residue | Details |
A | LEU108-PRO121 |