5XVV
Crystal Structure of Forward Inhibited Aspergillus niger Glutamate Dehydrogenase With Both Apo- and Alpha Ketoglutarate Bound Subunits
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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| D | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006537 | biological_process | glutamate biosynthetic 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 | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| E | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006537 | biological_process | glutamate biosynthetic 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 | 0004353 | molecular_function | glutamate dehydrogenase [NAD(P)+] activity |
| F | 0004354 | molecular_function | glutamate dehydrogenase (NADP+) activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0006537 | biological_process | glutamate biosynthetic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | SER72 |
| C | TRP176 |
| A | PRO76 |
| A | TYR77 |
| A | ASP147 |
| A | THR148 |
| A | HOH607 |
| C | ARG170 |
| C | ASN174 |
| C | GLN175 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ARG170 |
| A | ASN174 |
| A | GLN175 |
| A | TRP176 |
| B | SER72 |
| B | TYR77 |
| B | THR148 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | LEU105 |
| A | GLY107 |
| A | ASP414 |
| A | ASN418 |
| A | LYS448 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ALA427 |
| A | THR428 |
| A | HOH603 |
| A | HOH616 |
| A | HOH670 |
| B | VAL308 |
| B | GLU329 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ALA13 |
| A | GLU98 |
| A | LYS376 |
| A | ASN442 |
| A | HOH666 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | GLN48 |
| A | PHE49 |
| A | ARG50 |
| A | ARG64 |
| E | VAL42 |
| E | PRO43 |
| E | LYS93 |
| E | HOH622 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | GLY221 |
| A | GLY244 |
| D | ASN335 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue AKG A 508 |
| Chain | Residue |
| A | LYS78 |
| A | GLY80 |
| A | GLN99 |
| A | LYS102 |
| A | LYS114 |
| A | ALA152 |
| A | ARG193 |
| A | ASN346 |
| A | SER386 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue BME A 509 |
| Chain | Residue |
| A | THR138 |
| A | CYS141 |
| A | LYS142 |
| A | ILE172 |
| F | ILE172 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| A | GLY178 |
| A | SER394 |
| A | ARG396 |
| A | HOH706 |
| B | ASP147 |
| B | HOH663 |
| B | HOH698 |
| C | ARG396 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ASN174 |
| C | HIS143 |
| C | HOH736 |
| D | HOH689 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| A | ASN174 |
| A | GLN175 |
| B | LYS142 |
| B | HIS143 |
| B | ILE144 |
| B | THR148 |
| B | ARG173 |
| B | GOL504 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | LYS142 |
| B | GOL503 |
| B | HOH627 |
| B | HOH647 |
| B | HOH688 |
| F | LYS142 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| A | LEU397 |
| A | SER398 |
| B | LEU108 |
| B | ARG407 |
| B | ASP410 |
| B | HOH604 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue AKG B 506 |
| Chain | Residue |
| B | LYS78 |
| B | GLY80 |
| B | GLN99 |
| B | LYS102 |
| B | LYS114 |
| B | ALA152 |
| B | THR181 |
| B | SER386 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 501 |
| Chain | Residue |
| C | LEU105 |
| C | ASP414 |
| C | CYS415 |
| C | ASN418 |
| C | LYS448 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | GLN48 |
| C | PHE49 |
| C | ARG50 |
| C | ARG64 |
| D | VAL42 |
| D | PRO43 |
| D | LYS93 |
| D | HOH635 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| A | ARG407 |
| C | GLU403 |
| C | ARG407 |
| C | HOH712 |
| site_id | AE1 |
| Number of Residues | 11 |
| Details | binding site for residue AKG C 504 |
| Chain | Residue |
| C | LYS78 |
| C | GLY80 |
| C | GLN99 |
| C | LYS102 |
| C | LYS114 |
| C | ALA152 |
| C | ARG193 |
| C | VAL383 |
| C | SER386 |
| C | HOH672 |
| C | HOH742 |
| site_id | AE2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL E 501 |
| Chain | Residue |
| A | VAL42 |
| A | PRO43 |
| A | LYS93 |
| A | HOH693 |
| E | GLN48 |
| E | PHE49 |
| E | ARG50 |
| E | ARG64 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL E 502 |
| Chain | Residue |
| E | TYR199 |
| E | GLU242 |
| E | ASP405 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL E 503 |
| Chain | Residue |
| A | LYS142 |
| A | HIS143 |
| E | LYS142 |
| E | HOH633 |
| E | HOH672 |
| E | HOH704 |
| F | ASN174 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL E 504 |
| Chain | Residue |
| E | ARG361 |
| E | THR362 |
| E | HOH680 |
| E | HOH696 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue BME E 505 |
| Chain | Residue |
| C | ILE172 |
| E | CYS141 |
| E | LYS142 |
| E | ILE172 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL F 501 |
| Chain | Residue |
| F | ARG361 |
| F | THR362 |
| F | ALA427 |
| F | HOH665 |
| F | HOH675 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL F 502 |
| Chain | Residue |
| F | ALA210 |
| F | ARG413 |
| F | HOH691 |
| site_id | AE9 |
| Number of Residues | 10 |
| Details | binding site for residue GOL F 503 |
| Chain | Residue |
| A | GLU54 |
| A | ASP55 |
| A | ASP56 |
| A | GLY58 |
| A | ARG131 |
| F | GLU54 |
| F | ASP55 |
| F | ASP56 |
| F | GLY58 |
| F | ARG131 |
| site_id | AF1 |
| Number of Residues | 3 |
| Details | binding site for residue BME F 504 |
| Chain | Residue |
| A | ILE172 |
| F | CYS141 |
| F | ILE172 |
| site_id | AF2 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide BME B 507 and CYS B 141 |
| Chain | Residue |
| B | MET137 |
| B | THR138 |
| B | GLU139 |
| B | LEU140 |
| B | LYS142 |
| B | HIS143 |
| B | ILE144 |
| B | TYR169 |
| B | ILE172 |
| B | ARG173 |
| D | ILE172 |
| D | BME501 |
| site_id | AF3 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide BME C 505 and CYS C 141 |
| Chain | Residue |
| C | MET137 |
| C | THR138 |
| C | GLU139 |
| C | LEU140 |
| C | LYS142 |
| C | HIS143 |
| C | ILE144 |
| C | TYR169 |
| C | ARG173 |
| E | ILE172 |
| site_id | AF4 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide BME D 501 and CYS D 141 |
| Chain | Residue |
| B | ILE172 |
| B | BME507 |
| D | MET137 |
| D | THR138 |
| D | GLU139 |
| D | LEU140 |
| D | LYS142 |
| D | HIS143 |
| D | ILE144 |
| D | TYR169 |
| D | ILE172 |
| D | ARG173 |
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 |
