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 | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
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 | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
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 | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
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 |