7ECR
Crystal Structure of Aspergillus terreus Glutamate Dehydrogenase (AtGDH) Complexed With Succinate and ADP-ribose
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 | 8 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | ARG142 |
A | ILE144 |
A | THR148 |
A | GOL505 |
A | GOL505 |
A | HOH613 |
A | HOH660 |
B | ASN174 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | ARG407 |
A | HOH648 |
A | HOH884 |
A | HOH954 |
A | TRP399 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | LEU105 |
A | SER414 |
A | ASN418 |
A | LYS448 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | SER398 |
A | GLU403 |
A | HOH630 |
A | HOH648 |
A | HOH839 |
C | ARG407 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | ARG142 |
A | ARG142 |
A | HIS143 |
A | GOL501 |
A | GOL501 |
A | HOH603 |
A | HOH603 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue SIN A 506 |
Chain | Residue |
A | LYS78 |
A | GLY79 |
A | GLY80 |
A | GLN99 |
A | LYS102 |
A | LYS114 |
A | ALA152 |
A | ARG193 |
A | ASN379 |
A | VAL383 |
A | SER386 |
A | HOH654 |
A | HOH820 |
site_id | AC7 |
Number of Residues | 34 |
Details | binding site for residue A2R A 507 |
Chain | Residue |
A | ARG82 |
A | HIS84 |
A | LYS122 |
A | ASP154 |
A | ILE155 |
A | GLY156 |
A | SER229 |
A | GLY230 |
A | ASN231 |
A | VAL232 |
A | ASP252 |
A | SER253 |
A | LYS279 |
A | GLN284 |
A | SER319 |
A | ALA320 |
A | THR321 |
A | GLY344 |
A | SER345 |
A | ASN346 |
A | ASN379 |
A | HOH601 |
A | HOH610 |
A | HOH654 |
A | HOH664 |
A | HOH679 |
A | HOH690 |
A | HOH753 |
A | HOH800 |
A | HOH821 |
A | HOH826 |
A | HOH832 |
A | HOH876 |
A | HOH922 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 508 |
Chain | Residue |
A | GLN12 |
A | ASN323 |
A | THR350 |
A | GLN351 |
A | HOH784 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
B | TRP399 |
B | GLU403 |
B | ARG407 |
B | GOL503 |
B | HOH615 |
B | HOH788 |
B | HOH923 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | LEU105 |
B | SER414 |
B | ASN418 |
B | LYS448 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
A | ARG407 |
B | SER398 |
B | GLU403 |
B | GOL501 |
B | HOH659 |
B | HOH788 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | ARG142 |
B | ILE144 |
B | THR148 |
B | HOH601 |
C | ASN174 |
C | GOL506 |
C | HOH832 |
site_id | AD4 |
Number of Residues | 13 |
Details | binding site for residue SIN B 505 |
Chain | Residue |
B | LYS78 |
B | GLY79 |
B | GLY80 |
B | GLN99 |
B | LYS102 |
B | LYS114 |
B | ALA152 |
B | ARG193 |
B | ASN379 |
B | VAL383 |
B | SER386 |
B | HOH627 |
B | HOH808 |
site_id | AD5 |
Number of Residues | 35 |
Details | binding site for residue A2R B 506 |
Chain | Residue |
B | ARG82 |
B | HIS84 |
B | LYS122 |
B | ASP154 |
B | ILE155 |
B | GLY156 |
B | SER229 |
B | GLY230 |
B | ASN231 |
B | VAL232 |
B | SER251 |
B | ASP252 |
B | SER253 |
B | LYS279 |
B | GLN284 |
B | SER319 |
B | ALA320 |
B | THR321 |
B | GLY344 |
B | SER345 |
B | ASN346 |
B | ASN379 |
B | HOH627 |
B | HOH668 |
B | HOH675 |
B | HOH686 |
B | HOH707 |
B | HOH711 |
B | HOH722 |
B | HOH737 |
B | HOH759 |
B | HOH819 |
B | HOH846 |
B | HOH861 |
B | HOH864 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue GOL B 507 |
Chain | Residue |
B | GLN12 |
B | ASN323 |
B | THR350 |
B | GLN351 |
B | HOH684 |
B | HOH806 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 508 |
Chain | Residue |
B | GLU217 |
B | ALA220 |
B | GLY221 |
B | LYS222 |
B | HOH712 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue GOL C 501 |
Chain | Residue |
A | ASN174 |
C | ARG142 |
C | ILE144 |
C | THR148 |
C | GOL506 |
C | HOH604 |
C | HOH649 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
C | TRP399 |
C | GLU403 |
C | ARG407 |
C | GOL504 |
C | HOH616 |
C | HOH709 |
C | HOH884 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
C | LEU105 |
C | GLY107 |
C | SER414 |
C | ASN418 |
C | LYS448 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue GOL C 504 |
Chain | Residue |
B | ARG407 |
C | SER398 |
C | TRP399 |
C | GLU403 |
C | GOL502 |
C | HOH709 |
site_id | AE3 |
Number of Residues | 12 |
Details | binding site for residue GOL C 505 |
Chain | Residue |
C | HIS211 |
C | LYS365 |
C | GLY366 |
C | ASP431 |
C | GLY432 |
C | GLY432 |
C | ILE433 |
C | PRO435 |
C | HOH639 |
C | HOH639 |
C | HOH823 |
C | HOH868 |
site_id | AE4 |
Number of Residues | 7 |
Details | binding site for residue GOL C 506 |
Chain | Residue |
B | ARG142 |
B | GOL504 |
C | ARG142 |
C | HIS143 |
C | GOL501 |
C | HOH640 |
C | HOH658 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue GOL C 507 |
Chain | Residue |
C | ASP252 |
C | SER253 |
C | GLY303 |
C | GLN304 |
C | HOH603 |
C | HOH812 |
site_id | AE6 |
Number of Residues | 13 |
Details | binding site for residue SIN C 508 |
Chain | Residue |
C | LYS78 |
C | GLY79 |
C | GLY80 |
C | GLN99 |
C | LYS102 |
C | LYS114 |
C | ALA152 |
C | ARG193 |
C | ASN379 |
C | VAL383 |
C | SER386 |
C | HOH675 |
C | HOH787 |
site_id | AE7 |
Number of Residues | 34 |
Details | binding site for residue A2R C 509 |
Chain | Residue |
C | ARG82 |
C | HIS84 |
C | LYS122 |
C | ASP154 |
C | ILE155 |
C | GLY156 |
C | SER229 |
C | GLY230 |
C | ASN231 |
C | VAL232 |
C | ASP252 |
C | SER253 |
C | LYS279 |
C | GLN284 |
C | SER319 |
C | ALA320 |
C | THR321 |
C | GLY344 |
C | SER345 |
C | ASN346 |
C | ASN379 |
C | HOH632 |
C | HOH654 |
C | HOH675 |
C | HOH718 |
C | HOH719 |
C | HOH742 |
C | HOH791 |
C | HOH804 |
C | HOH814 |
C | HOH838 |
C | HOH874 |
C | HOH880 |
C | HOH926 |
site_id | AE8 |
Number of Residues | 5 |
Details | binding site for residue GOL C 510 |
Chain | Residue |
C | GLN12 |
C | ASN323 |
C | GLN351 |
C | HOH621 |
C | HOH829 |
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 |