6S6S
Structure of Azospirillum brasilense Glutamate Synthase in a4b4 oligomeric state.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| A | 0006537 | biological_process | glutamate biosynthetic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0015930 | molecular_function | glutamate synthase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| A | 0019676 | biological_process | ammonia assimilation cycle |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| A | 0097054 | biological_process | L-glutamate biosynthetic process |
| B | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| B | 0006537 | biological_process | glutamate biosynthetic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0015930 | molecular_function | glutamate synthase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| B | 0019676 | biological_process | ammonia assimilation cycle |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| B | 0097054 | biological_process | L-glutamate biosynthetic process |
| C | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| C | 0006537 | biological_process | glutamate biosynthetic process |
| C | 0006541 | biological_process | glutamine metabolic process |
| C | 0015930 | molecular_function | glutamate synthase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| C | 0019676 | biological_process | ammonia assimilation cycle |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| C | 0097054 | biological_process | L-glutamate biosynthetic process |
| D | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| D | 0006537 | biological_process | glutamate biosynthetic process |
| D | 0006541 | biological_process | glutamine metabolic process |
| D | 0015930 | molecular_function | glutamate synthase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| D | 0019676 | biological_process | ammonia assimilation cycle |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| D | 0097054 | biological_process | L-glutamate biosynthetic process |
| E | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| E | 0006537 | biological_process | glutamate biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 0097054 | biological_process | L-glutamate biosynthetic process |
| F | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| F | 0006537 | biological_process | glutamate biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 0097054 | biological_process | L-glutamate biosynthetic process |
| G | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| G | 0006537 | biological_process | glutamate biosynthetic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051536 | molecular_function | iron-sulfur cluster binding |
| G | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| G | 0097054 | biological_process | L-glutamate biosynthetic process |
| H | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| H | 0006537 | biological_process | glutamate biosynthetic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051536 | molecular_function | iron-sulfur cluster binding |
| H | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| H | 0097054 | biological_process | L-glutamate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue FMN A 1501 |
| Chain | Residue |
| A | PRO856 |
| A | SER1027 |
| A | GLY1028 |
| A | GLY1029 |
| A | THR1030 |
| A | ASP1070 |
| A | GLY1071 |
| A | GLY1072 |
| A | ILE1092 |
| A | GLY1093 |
| A | THR1094 |
| A | GLY857 |
| A | MET858 |
| A | SER859 |
| A | GLU886 |
| A | GLN909 |
| A | LYS931 |
| A | GLN934 |
| A | LYS999 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue F3S A 1502 |
| Chain | Residue |
| A | MET479 |
| A | CYS1102 |
| A | ILE1103 |
| A | MET1104 |
| A | VAL1105 |
| A | ARG1106 |
| A | CYS1108 |
| A | CYS1113 |
| A | VAL1115 |
| A | VAL1117 |
| A | CYS1118 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue FMN B 1501 |
| Chain | Residue |
| B | PRO856 |
| B | GLY857 |
| B | MET858 |
| B | SER859 |
| B | LYS931 |
| B | LYS999 |
| B | SER1024 |
| B | GLY1028 |
| B | GLY1029 |
| B | THR1030 |
| B | ASP1070 |
| B | GLY1071 |
| B | GLY1072 |
| B | ILE1092 |
| B | GLY1093 |
| B | THR1094 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue F3S B 1502 |
| Chain | Residue |
| B | MET479 |
| B | CYS1102 |
| B | MET1104 |
| B | VAL1105 |
| B | ARG1106 |
| B | GLN1107 |
| B | CYS1108 |
| B | CYS1113 |
| B | CYS1118 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue FMN C 1501 |
| Chain | Residue |
| C | PRO856 |
| C | GLY857 |
| C | MET858 |
| C | SER859 |
| C | GLU886 |
| C | GLN909 |
| C | LYS931 |
| C | LYS999 |
| C | GLY1028 |
| C | GLY1029 |
| C | THR1030 |
| C | GLY1071 |
| C | GLY1072 |
| C | ILE1092 |
| C | GLY1093 |
| C | THR1094 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue FMN D 1501 |
| Chain | Residue |
| D | PRO856 |
| D | GLY857 |
| D | MET858 |
| D | SER859 |
| D | LYS931 |
| D | LYS999 |
| D | SER1027 |
| D | GLY1028 |
| D | GLY1029 |
| D | THR1030 |
| D | ASP1070 |
| D | GLY1071 |
| D | GLY1072 |
| D | GLY1093 |
| D | THR1094 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue F3S D 1502 |
| Chain | Residue |
| D | CYS1102 |
| D | ILE1103 |
| D | MET1104 |
| D | VAL1105 |
| D | ARG1106 |
| D | CYS1108 |
| D | CYS1113 |
| D | VAL1117 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 G 501 |
| Chain | Residue |
| G | PHE55 |
| G | CYS56 |
| G | CYS109 |
| G | VAL110 |
| G | CYS48 |
| G | SER49 |
| G | GLN50 |
| G | CYS51 |
| G | PRO54 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | binding site for residue FAD G 503 |
| Chain | Residue |
| G | ILE98 |
| G | GLY155 |
| G | ALA156 |
| G | GLY157 |
| G | PRO158 |
| G | ALA159 |
| G | ASP178 |
| G | ARG179 |
| G | TYR180 |
| G | GLY185 |
| G | LEU186 |
| G | ILE191 |
| G | VAL221 |
| G | THR241 |
| G | GLY242 |
| G | TYR244 |
| G | ASP300 |
| G | ASP443 |
| G | SER449 |
| G | LEU450 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 E 501 |
| Chain | Residue |
| E | CYS48 |
| E | SER49 |
| E | CYS51 |
| E | CYS56 |
| E | CYS109 |
| E | VAL110 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 E 502 |
| Chain | Residue |
| E | CYS60 |
| E | PRO61 |
| E | ILE66 |
| E | CYS95 |
| E | CYS99 |
| E | CYS105 |
| E | GLU125 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for residue FAD E 503 |
| Chain | Residue |
| E | ILE98 |
| E | ILE154 |
| E | GLY155 |
| E | GLY157 |
| E | PRO158 |
| E | ASP178 |
| E | ARG179 |
| E | TYR180 |
| E | GLY185 |
| E | LEU186 |
| E | ILE191 |
| E | LYS195 |
| E | VAL221 |
| E | ALA240 |
| E | THR241 |
| E | GLY242 |
| E | TYR244 |
| E | ASP304 |
| E | ASP443 |
| E | SER449 |
| E | LEU450 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 F 501 |
| Chain | Residue |
| F | CYS48 |
| F | SER49 |
| F | GLN50 |
| F | CYS51 |
| F | CYS56 |
| F | CYS109 |
| F | VAL110 |
| F | ILE111 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 F 502 |
| Chain | Residue |
| F | CYS60 |
| F | ASN64 |
| F | ASN89 |
| F | CYS95 |
| F | GLY96 |
| F | CYS99 |
| F | CYS105 |
| F | GLU125 |
| site_id | AD6 |
| Number of Residues | 23 |
| Details | binding site for residue FAD F 503 |
| Chain | Residue |
| F | ILE98 |
| F | ILE154 |
| F | GLY155 |
| F | ALA156 |
| F | GLY157 |
| F | PRO158 |
| F | ALA159 |
| F | ASP178 |
| F | ARG179 |
| F | TYR180 |
| F | GLY185 |
| F | LEU186 |
| F | ILE191 |
| F | VAL221 |
| F | ALA240 |
| F | THR241 |
| F | GLY242 |
| F | TYR244 |
| F | ASP300 |
| F | GLY442 |
| F | ASP443 |
| F | SER449 |
| F | LEU450 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 H 501 |
| Chain | Residue |
| H | CYS48 |
| H | SER49 |
| H | CYS51 |
| H | CYS56 |
| H | CYS109 |
| H | VAL110 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue SF4 H 502 |
| Chain | Residue |
| H | CYS60 |
| H | CYS99 |
| H | CYS105 |
| H | GLU125 |
| site_id | AD9 |
| Number of Residues | 18 |
| Details | binding site for residue FAD H 503 |
| Chain | Residue |
| H | ILE98 |
| H | GLY155 |
| H | ALA156 |
| H | GLY157 |
| H | PRO158 |
| H | ALA159 |
| H | ASP178 |
| H | ARG179 |
| H | TYR180 |
| H | LEU186 |
| H | ILE191 |
| H | PHE219 |
| H | ALA240 |
| H | THR241 |
| H | GLY242 |
| H | ASP300 |
| H | ASP443 |
| H | SER449 |
| site_id | AE1 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide F3S C 1502 and CYS C 1108 |
| Chain | Residue |
| C | MET479 |
| C | CYS1102 |
| C | ILE1103 |
| C | MET1104 |
| C | VAL1105 |
| C | ARG1106 |
| C | GLN1107 |
| C | HIS1109 |
| C | SER1110 |
| C | CYS1113 |
| C | CYS1118 |
| site_id | AE2 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide SF4 G 502 and CYS G 105 |
| Chain | Residue |
| G | CYS60 |
| G | ASN64 |
| G | CYS99 |
| G | LEU104 |
| G | GLU106 |
| G | GLY107 |
| G | ASN108 |
| G | CYS109 |
| G | ILE121 |
| G | GLU125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| G | CYS95 | |
| F | CYS99 | |
| F | CYS105 | |
| F | CYS109 | |
| H | CYS95 | |
| H | CYS99 | |
| H | CYS105 | |
| H | CYS109 | |
| G | CYS99 | |
| G | CYS105 | |
| G | CYS109 | |
| E | CYS95 | |
| E | CYS99 | |
| E | CYS105 | |
| E | CYS109 | |
| F | CYS95 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LEU1049 | |
| B | CYS1113 | |
| C | LEU1049 | |
| C | SER1050 | |
| C | CYS1102 | |
| C | CYS1108 | |
| C | CYS1113 | |
| D | LEU1049 | |
| D | SER1050 | |
| D | CYS1102 | |
| D | CYS1108 | |
| A | SER1050 | |
| D | CYS1113 | |
| A | CYS1102 | |
| A | CYS1108 | |
| A | CYS1113 | |
| B | LEU1049 | |
| B | SER1050 | |
| B | CYS1102 | |
| B | CYS1108 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| A | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| A | MET479 | single electron acceptor, single electron donor, single electron relay |
| A | GLU886 | proton acceptor, proton donor, proton relay |
| A | LYS937 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| B | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| B | MET479 | single electron acceptor, single electron donor, single electron relay |
| B | GLU886 | proton acceptor, proton donor, proton relay |
| B | LYS937 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| C | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| C | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| C | MET479 | single electron acceptor, single electron donor, single electron relay |
| C | GLU886 | proton acceptor, proton donor, proton relay |
| C | LYS937 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| D | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| D | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| D | MET479 | single electron acceptor, single electron donor, single electron relay |
| D | GLU886 | proton acceptor, proton donor, proton relay |
| D | LYS937 | electrostatic stabiliser |
