6S6X
Structure of Azospirillum brasilense Glutamate Synthase in a6b6 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 | 0008652 | biological_process | amino acid biosynthetic 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 | 0051536 | molecular_function | iron-sulfur cluster 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 | 0008652 | biological_process | amino acid biosynthetic 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 | 0051536 | molecular_function | iron-sulfur cluster 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 | 0008652 | biological_process | amino acid biosynthetic 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 | 0051536 | molecular_function | iron-sulfur cluster 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 | 0008652 | biological_process | amino acid biosynthetic 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 | 0051536 | molecular_function | iron-sulfur cluster 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 | 0008652 | biological_process | amino acid biosynthetic process |
| E | 0015930 | molecular_function | glutamate synthase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| E | 0019676 | biological_process | ammonia assimilation cycle |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051538 | molecular_function | 3 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 | 0008652 | biological_process | amino acid biosynthetic process |
| F | 0015930 | molecular_function | glutamate synthase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| F | 0019676 | biological_process | ammonia assimilation cycle |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051538 | molecular_function | 3 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 | 0008652 | biological_process | amino acid 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 | 0008652 | biological_process | amino acid 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 |
| I | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| I | 0006537 | biological_process | glutamate biosynthetic process |
| I | 0008652 | biological_process | amino acid biosynthetic process |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051536 | molecular_function | iron-sulfur cluster binding |
| I | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| I | 0097054 | biological_process | L-glutamate biosynthetic process |
| J | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| J | 0006537 | biological_process | glutamate biosynthetic process |
| J | 0008652 | biological_process | amino acid biosynthetic process |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0051536 | molecular_function | iron-sulfur cluster binding |
| J | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| J | 0097054 | biological_process | L-glutamate biosynthetic process |
| K | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| K | 0006537 | biological_process | glutamate biosynthetic process |
| K | 0008652 | biological_process | amino acid biosynthetic process |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0051536 | molecular_function | iron-sulfur cluster binding |
| K | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| K | 0097054 | biological_process | L-glutamate biosynthetic process |
| L | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
| L | 0006537 | biological_process | glutamate biosynthetic process |
| L | 0008652 | biological_process | amino acid biosynthetic process |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051536 | molecular_function | iron-sulfur cluster binding |
| L | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| L | 0097054 | biological_process | L-glutamate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue FMN A 1501 |
| Chain | Residue |
| A | PRO856 |
| A | THR1030 |
| A | ASP1070 |
| A | GLY1071 |
| A | GLY1072 |
| A | ILE1092 |
| A | GLY1093 |
| A | THR1094 |
| A | GLY857 |
| A | SER859 |
| A | GLU886 |
| A | GLN909 |
| A | LYS931 |
| A | LYS999 |
| A | GLY1028 |
| A | GLY1029 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue F3S A 1502 |
| Chain | Residue |
| A | CYS1102 |
| A | MET1104 |
| A | VAL1105 |
| A | ARG1106 |
| A | GLN1107 |
| A | CYS1108 |
| A | CYS1113 |
| A | CYS1118 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue FMN B 1501 |
| Chain | Residue |
| B | PRO856 |
| B | GLY857 |
| B | MET858 |
| B | SER859 |
| B | GLU886 |
| B | GLN909 |
| B | LYS931 |
| B | GLN934 |
| B | LYS999 |
| B | GLY1028 |
| B | GLY1029 |
| B | THR1030 |
| B | GLY1071 |
| B | GLY1072 |
| B | ILE1092 |
| B | GLY1093 |
| B | THR1094 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue F3S B 1502 |
| Chain | Residue |
| B | CYS1102 |
| B | MET1104 |
| B | VAL1105 |
| B | ARG1106 |
| B | GLN1107 |
| B | CYS1108 |
| B | CYS1113 |
| B | CYS1118 |
| site_id | AC5 |
| Number of Residues | 19 |
| 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 | GLN934 |
| C | LYS999 |
| C | SER1027 |
| C | GLY1028 |
| C | GLY1029 |
| C | THR1030 |
| C | ASP1070 |
| C | GLY1071 |
| C | GLY1072 |
| C | ILE1092 |
| C | GLY1093 |
| C | THR1094 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue F3S C 1502 |
| Chain | Residue |
| C | CYS1102 |
| C | ILE1103 |
| C | MET1104 |
| C | VAL1105 |
| C | ARG1106 |
| C | GLN1107 |
| C | CYS1108 |
| C | CYS1113 |
| C | CYS1118 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue FMN D 1501 |
| Chain | Residue |
| D | PRO856 |
| D | GLY857 |
| D | SER859 |
| D | GLU886 |
| D | GLN909 |
| D | LYS931 |
| D | LYS999 |
| D | GLY1028 |
| D | GLY1029 |
| D | THR1030 |
| D | ASP1070 |
| D | GLY1071 |
| D | GLY1072 |
| D | ILE1092 |
| D | GLY1093 |
| D | THR1094 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue F3S D 1502 |
| Chain | Residue |
| D | CYS1113 |
| D | CYS1118 |
| D | CYS1102 |
| D | MET1104 |
| D | VAL1105 |
| D | ARG1106 |
| D | GLN1107 |
| D | CYS1108 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | binding site for residue FMN E 1501 |
| Chain | Residue |
| E | PRO856 |
| E | GLY857 |
| E | MET858 |
| E | SER859 |
| E | GLU886 |
| E | GLN909 |
| E | LYS931 |
| E | GLN934 |
| E | LYS999 |
| E | GLY1028 |
| E | GLY1029 |
| E | THR1030 |
| E | GLY1071 |
| E | GLY1072 |
| E | ILE1092 |
| E | GLY1093 |
| E | THR1094 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue F3S E 1502 |
| Chain | Residue |
| E | CYS1102 |
| E | MET1104 |
| E | VAL1105 |
| E | ARG1106 |
| E | GLN1107 |
| E | CYS1108 |
| E | CYS1113 |
| E | CYS1118 |
| site_id | AD2 |
| Number of Residues | 19 |
| Details | binding site for residue FMN F 1501 |
| Chain | Residue |
| F | PRO856 |
| F | GLY857 |
| F | MET858 |
| F | SER859 |
| F | GLU886 |
| F | GLN909 |
| F | LYS931 |
| F | GLN934 |
| F | LYS999 |
| F | SER1027 |
| F | GLY1028 |
| F | GLY1029 |
| F | THR1030 |
| F | ASP1070 |
| F | GLY1071 |
| F | GLY1072 |
| F | ILE1092 |
| F | GLY1093 |
| F | THR1094 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue F3S F 1502 |
| Chain | Residue |
| F | CYS1102 |
| F | ILE1103 |
| F | MET1104 |
| F | VAL1105 |
| F | ARG1106 |
| F | GLN1107 |
| F | CYS1108 |
| F | CYS1113 |
| F | CYS1118 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 G 501 |
| Chain | Residue |
| G | CYS48 |
| G | SER49 |
| G | CYS51 |
| G | CYS56 |
| G | PRO67 |
| G | CYS109 |
| G | VAL110 |
| G | VAL119 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 G 502 |
| Chain | Residue |
| G | CYS60 |
| G | ASN64 |
| G | CYS95 |
| G | CYS99 |
| G | GLN101 |
| G | CYS105 |
| G | GLU125 |
| site_id | AD6 |
| Number of Residues | 20 |
| Details | binding site for residue FAD G 503 |
| Chain | Residue |
| G | ILE98 |
| G | GLY157 |
| G | PRO158 |
| G | ALA159 |
| G | ASP178 |
| G | ARG179 |
| G | GLY185 |
| G | LEU186 |
| G | GLU220 |
| G | VAL221 |
| G | THR241 |
| G | GLY242 |
| G | TYR244 |
| G | ASP300 |
| G | THR301 |
| G | ASP304 |
| G | PHE402 |
| G | ASP443 |
| G | SER449 |
| G | LEU450 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 H 501 |
| Chain | Residue |
| H | CYS48 |
| H | SER49 |
| H | CYS51 |
| H | CYS56 |
| H | PRO67 |
| H | CYS109 |
| H | VAL110 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 H 502 |
| Chain | Residue |
| H | CYS60 |
| H | ASN64 |
| H | ILE66 |
| H | CYS99 |
| H | CYS105 |
| H | ILE121 |
| H | GLU125 |
| site_id | AD9 |
| Number of Residues | 20 |
| Details | binding site for residue FAD H 503 |
| Chain | Residue |
| H | ILE98 |
| H | GLY155 |
| H | GLY157 |
| H | PRO158 |
| H | TYR177 |
| H | ASP178 |
| H | ARG179 |
| H | TYR180 |
| H | GLY185 |
| H | LEU186 |
| H | LYS195 |
| H | GLU220 |
| H | VAL221 |
| H | THR241 |
| H | ASP300 |
| H | THR301 |
| H | ASP304 |
| H | ASP443 |
| H | SER449 |
| H | VAL451 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 I 501 |
| Chain | Residue |
| I | CYS48 |
| I | SER49 |
| I | CYS51 |
| I | CYS56 |
| I | PRO67 |
| I | CYS109 |
| I | VAL110 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 I 502 |
| Chain | Residue |
| I | CYS60 |
| I | ASN64 |
| I | ILE66 |
| I | CYS99 |
| I | CYS105 |
| I | GLU125 |
| site_id | AE3 |
| Number of Residues | 23 |
| Details | binding site for residue FAD I 503 |
| Chain | Residue |
| I | ILE98 |
| I | GLY155 |
| I | ALA156 |
| I | GLY157 |
| I | PRO158 |
| I | ALA159 |
| I | TYR177 |
| I | ASP178 |
| I | ARG179 |
| I | TYR180 |
| I | GLY185 |
| I | LEU186 |
| I | LYS195 |
| I | GLU220 |
| I | VAL221 |
| I | THR241 |
| I | TYR244 |
| I | ASP300 |
| I | ASP304 |
| I | ASP443 |
| I | SER449 |
| I | VAL451 |
| I | ALA454 |
| site_id | AE4 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 J 501 |
| Chain | Residue |
| J | CYS48 |
| J | SER49 |
| J | CYS51 |
| J | CYS56 |
| J | PRO67 |
| J | CYS109 |
| J | VAL110 |
| J | VAL119 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 J 502 |
| Chain | Residue |
| J | CYS60 |
| J | ASN64 |
| J | CYS95 |
| J | CYS99 |
| J | GLN101 |
| J | CYS105 |
| J | GLU125 |
| site_id | AE6 |
| Number of Residues | 22 |
| Details | binding site for residue FAD J 503 |
| Chain | Residue |
| J | ILE98 |
| J | ILE154 |
| J | GLY155 |
| J | GLY157 |
| J | PRO158 |
| J | ALA159 |
| J | TYR177 |
| J | ASP178 |
| J | ARG179 |
| J | TYR180 |
| J | GLY185 |
| J | LEU186 |
| J | GLU220 |
| J | VAL221 |
| J | THR241 |
| J | GLY242 |
| J | TYR244 |
| J | ASP300 |
| J | ASP304 |
| J | PHE402 |
| J | ASP443 |
| J | SER449 |
| site_id | AE7 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 K 501 |
| Chain | Residue |
| K | CYS48 |
| K | SER49 |
| K | CYS51 |
| K | CYS56 |
| K | PRO67 |
| K | CYS109 |
| K | VAL110 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 K 502 |
| Chain | Residue |
| K | CYS60 |
| K | ASN64 |
| K | ILE66 |
| K | CYS99 |
| K | CYS105 |
| K | ILE121 |
| K | GLU125 |
| site_id | AE9 |
| Number of Residues | 20 |
| Details | binding site for residue FAD K 503 |
| Chain | Residue |
| K | ILE98 |
| K | GLY157 |
| K | PRO158 |
| K | ALA159 |
| K | TYR177 |
| K | ASP178 |
| K | ARG179 |
| K | TYR180 |
| K | LEU186 |
| K | LYS195 |
| K | GLU220 |
| K | VAL221 |
| K | THR241 |
| K | TYR244 |
| K | ASP300 |
| K | ASP304 |
| K | ASP443 |
| K | SER449 |
| K | VAL451 |
| K | ALA454 |
| site_id | AF1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 L 501 |
| Chain | Residue |
| L | CYS48 |
| L | SER49 |
| L | CYS51 |
| L | CYS56 |
| L | PRO67 |
| L | CYS109 |
| L | VAL110 |
| site_id | AF2 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 L 502 |
| Chain | Residue |
| L | CYS60 |
| L | ASN64 |
| L | ILE66 |
| L | CYS99 |
| L | CYS105 |
| L | GLU125 |
| site_id | AF3 |
| Number of Residues | 20 |
| Details | binding site for residue FAD L 503 |
| Chain | Residue |
| L | ILE98 |
| L | GLY155 |
| L | GLY157 |
| L | PRO158 |
| L | TYR177 |
| L | ASP178 |
| L | ARG179 |
| L | TYR180 |
| L | GLY185 |
| L | LEU186 |
| L | GLU220 |
| L | VAL221 |
| L | THR241 |
| L | ASP300 |
| L | THR301 |
| L | ASP304 |
| L | PHE402 |
| L | ASP443 |
| L | SER449 |
| L | VAL451 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2370 |
| Details | Domain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 126 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 60 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Active site: {"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 696 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 198 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
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 |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| E | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| E | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| E | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| E | MET479 | single electron acceptor, single electron donor, single electron relay |
| E | GLU886 | proton acceptor, proton donor, proton relay |
| E | LYS937 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 304 |
| Chain | Residue | Details |
| F | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| F | ASN231 | electrostatic stabiliser, hydrogen bond donor |
| F | GLY232 | electrostatic stabiliser, hydrogen bond donor |
| F | MET479 | single electron acceptor, single electron donor, single electron relay |
| F | GLU886 | proton acceptor, proton donor, proton relay |
| F | LYS937 | electrostatic stabiliser |
