7ECT
Crystal Structure of Aspergillus terreus Glutamate Dehydrogenase (AtGDH) Complexed With Tartrate and NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006537 | biological_process | glutamate biosynthetic 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 | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006537 | biological_process | glutamate biosynthetic 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 | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006537 | biological_process | glutamate biosynthetic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue NDP A 501 |
| Chain | Residue |
| A | ARG82 |
| A | GLY230 |
| A | ASN231 |
| A | VAL232 |
| A | SER251 |
| A | ASP252 |
| A | SER253 |
| A | LYS279 |
| A | GLN284 |
| A | SER319 |
| A | ALA320 |
| A | LYS122 |
| A | THR321 |
| A | GLY344 |
| A | SER345 |
| A | ASN346 |
| A | ASN379 |
| A | GOL504 |
| A | GOL505 |
| A | TLA507 |
| A | HOH605 |
| A | ASP154 |
| A | ILE155 |
| A | GLY156 |
| A | ARG193 |
| A | THR197 |
| A | GLY228 |
| A | SER229 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ARG142 |
| A | ILE144 |
| A | THR148 |
| A | ARG173 |
| B | ASN174 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TRP399 |
| A | GLU403 |
| A | ARG407 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ASP252 |
| A | SER253 |
| A | GLN254 |
| A | GLY255 |
| A | GLN304 |
| A | NDP501 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | GLY153 |
| A | VAL157 |
| A | ARG193 |
| A | NDP501 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | GLN12 |
| A | THR350 |
| A | GLN351 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue TLA A 507 |
| Chain | Residue |
| A | LYS78 |
| A | GLY79 |
| A | GLY80 |
| A | GLN99 |
| A | LYS102 |
| A | LYS114 |
| A | ALA152 |
| A | GLY153 |
| A | THR181 |
| A | ARG193 |
| A | ASN346 |
| A | VAL383 |
| A | SER386 |
| A | NDP501 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | binding site for residue NDP B 501 |
| Chain | Residue |
| B | ARG82 |
| B | HIS84 |
| B | LYS122 |
| B | ASP154 |
| B | ILE155 |
| B | GLY156 |
| B | ARG193 |
| B | THR197 |
| B | SER229 |
| B | GLY230 |
| B | ASN231 |
| B | VAL232 |
| B | ASP252 |
| B | SER253 |
| B | LYS279 |
| B | GLN284 |
| B | SER319 |
| B | ALA320 |
| B | THR321 |
| B | GLY344 |
| B | SER345 |
| B | ASN346 |
| B | ASN379 |
| B | TLA503 |
| B | HOH602 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | TRP399 |
| B | GLU403 |
| B | ARG407 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for residue TLA B 503 |
| Chain | Residue |
| B | ASP154 |
| B | THR181 |
| B | ARG193 |
| B | ASN346 |
| B | VAL383 |
| B | SER386 |
| B | NDP501 |
| B | LYS78 |
| B | GLY79 |
| B | GLY80 |
| B | GLN99 |
| B | LYS102 |
| B | LYS114 |
| B | ALA152 |
| B | GLY153 |
| site_id | AD2 |
| Number of Residues | 24 |
| Details | binding site for residue NDP C 501 |
| Chain | Residue |
| C | ARG82 |
| C | HIS84 |
| C | LYS122 |
| C | GLY153 |
| C | ASP154 |
| C | ILE155 |
| C | GLY156 |
| C | ARG193 |
| C | THR197 |
| C | SER229 |
| C | GLY230 |
| C | ASN231 |
| C | VAL232 |
| C | ASP252 |
| C | SER253 |
| C | LYS279 |
| C | GLN284 |
| C | ALA320 |
| C | THR321 |
| C | GLY344 |
| C | SER345 |
| C | ASN346 |
| C | ASN379 |
| C | TLA508 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | TRP399 |
| C | GLU403 |
| C | ARG407 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| C | ASP252 |
| C | SER253 |
| C | GLY303 |
| C | GLN304 |
| C | ARG305 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 504 |
| Chain | Residue |
| B | ARG142 |
| B | ILE144 |
| B | THR148 |
| B | ARG173 |
| C | ARG142 |
| C | ASN174 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 505 |
| Chain | Residue |
| B | ARG142 |
| B | HIS143 |
| C | ARG142 |
| C | HIS143 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 506 |
| Chain | Residue |
| B | ASP147 |
| C | ALA146 |
| C | GLY178 |
| C | ASN393 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL C 507 |
| Chain | Residue |
| C | GLY244 |
| site_id | AD9 |
| Number of Residues | 14 |
| Details | binding site for residue TLA C 508 |
| Chain | Residue |
| C | LYS78 |
| C | GLY80 |
| C | GLN99 |
| C | LYS102 |
| C | LYS114 |
| C | ALA152 |
| C | GLY153 |
| C | ASP154 |
| C | ARG193 |
| C | ASN346 |
| C | GLY382 |
| C | VAL383 |
| C | SER386 |
| C | NDP501 |
Functional Information from PROSITE/UniProt
| site_id | PS00074 |
| Number of Residues | 14 |
| Details | GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LnmGGGKgGsdfDP |
| Chain | Residue | Details |
| A | LEU108-PRO121 |






