1OGY
Crystal structure of the heterodimeric nitrate reductase from Rhodobacter sphaeroides
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| A | 0008940 | molecular_function | nitrate reductase activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030151 | molecular_function | molybdenum ion binding |
| A | 0042128 | biological_process | nitrate assimilation |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0045333 | biological_process | cellular respiration |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 1990204 | cellular_component | oxidoreductase complex |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| C | 0008940 | molecular_function | nitrate reductase activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030151 | molecular_function | molybdenum ion binding |
| C | 0042128 | biological_process | nitrate assimilation |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0043546 | molecular_function | molybdopterin cofactor binding |
| C | 0045333 | biological_process | cellular respiration |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 1990204 | cellular_component | oxidoreductase complex |
| D | 0009061 | biological_process | anaerobic respiration |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| E | 0008940 | molecular_function | nitrate reductase activity |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0030151 | molecular_function | molybdenum ion binding |
| E | 0042128 | biological_process | nitrate assimilation |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0043546 | molecular_function | molybdopterin cofactor binding |
| E | 0045333 | biological_process | cellular respiration |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 1990204 | cellular_component | oxidoreductase complex |
| F | 0009061 | biological_process | anaerobic respiration |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| G | 0008940 | molecular_function | nitrate reductase activity |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0030151 | molecular_function | molybdenum ion binding |
| G | 0042128 | biological_process | nitrate assimilation |
| G | 0042597 | cellular_component | periplasmic space |
| G | 0043546 | molecular_function | molybdopterin cofactor binding |
| G | 0045333 | biological_process | cellular respiration |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| G | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| G | 1990204 | cellular_component | oxidoreductase complex |
| H | 0009061 | biological_process | anaerobic respiration |
| H | 0042597 | cellular_component | periplasmic space |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0005506 | molecular_function | iron ion binding |
| I | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| I | 0008940 | molecular_function | nitrate reductase activity |
| I | 0009055 | molecular_function | electron transfer activity |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0030151 | molecular_function | molybdenum ion binding |
| I | 0042128 | biological_process | nitrate assimilation |
| I | 0042597 | cellular_component | periplasmic space |
| I | 0043546 | molecular_function | molybdopterin cofactor binding |
| I | 0045333 | biological_process | cellular respiration |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| I | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| I | 1990204 | cellular_component | oxidoreductase complex |
| J | 0009061 | biological_process | anaerobic respiration |
| J | 0042597 | cellular_component | periplasmic space |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0005506 | molecular_function | iron ion binding |
| K | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| K | 0008940 | molecular_function | nitrate reductase activity |
| K | 0009055 | molecular_function | electron transfer activity |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0030151 | molecular_function | molybdenum ion binding |
| K | 0042128 | biological_process | nitrate assimilation |
| K | 0042597 | cellular_component | periplasmic space |
| K | 0043546 | molecular_function | molybdopterin cofactor binding |
| K | 0045333 | biological_process | cellular respiration |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| K | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| K | 1990204 | cellular_component | oxidoreductase complex |
| L | 0009061 | biological_process | anaerobic respiration |
| L | 0042597 | cellular_component | periplasmic space |
| L | 0046872 | molecular_function | metal ion binding |
| M | 0005506 | molecular_function | iron ion binding |
| M | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| M | 0008940 | molecular_function | nitrate reductase activity |
| M | 0009055 | molecular_function | electron transfer activity |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0030151 | molecular_function | molybdenum ion binding |
| M | 0042128 | biological_process | nitrate assimilation |
| M | 0042597 | cellular_component | periplasmic space |
| M | 0043546 | molecular_function | molybdopterin cofactor binding |
| M | 0045333 | biological_process | cellular respiration |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| M | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| M | 1990204 | cellular_component | oxidoreductase complex |
| N | 0009061 | biological_process | anaerobic respiration |
| N | 0042597 | cellular_component | periplasmic space |
| N | 0046872 | molecular_function | metal ion binding |
| O | 0005506 | molecular_function | iron ion binding |
| O | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| O | 0008940 | molecular_function | nitrate reductase activity |
| O | 0009055 | molecular_function | electron transfer activity |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0030151 | molecular_function | molybdenum ion binding |
| O | 0042128 | biological_process | nitrate assimilation |
| O | 0042597 | cellular_component | periplasmic space |
| O | 0043546 | molecular_function | molybdopterin cofactor binding |
| O | 0045333 | biological_process | cellular respiration |
| O | 0046872 | molecular_function | metal ion binding |
| O | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| O | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| O | 1990204 | cellular_component | oxidoreductase complex |
| P | 0009061 | biological_process | anaerobic respiration |
| P | 0042597 | cellular_component | periplasmic space |
| P | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 A1801 |
| Chain | Residue |
| A | CYS19 |
| A | CYS22 |
| A | CYS26 |
| A | CYS54 |
| A | GLY57 |
| A | PRO194 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO A1802 |
| Chain | Residue |
| A | CYS152 |
| A | MGD1803 |
| A | MGD1804 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD A1803 |
| Chain | Residue |
| A | ARG20 |
| A | GLN123 |
| A | ASN148 |
| A | CYS152 |
| A | GLN350 |
| A | GLN384 |
| A | VAL454 |
| A | ASN455 |
| A | ASN456 |
| A | ASN457 |
| A | ALA460 |
| A | SER482 |
| A | ASP483 |
| A | THR487 |
| A | ALA499 |
| A | ALA500 |
| A | MET501 |
| A | LYS505 |
| A | ASP532 |
| A | THR692 |
| A | ARG694 |
| A | TRP699 |
| A | HIS700 |
| A | SER701 |
| A | SER703 |
| A | TRP768 |
| A | ASN776 |
| A | PHE792 |
| A | LYS793 |
| A | MO1802 |
| A | MGD1804 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD A1804 |
| Chain | Residue |
| A | LYS56 |
| A | CYS152 |
| A | TRP185 |
| A | GLY186 |
| A | SER187 |
| A | ASN188 |
| A | GLU191 |
| A | MET192 |
| A | SER216 |
| A | THR217 |
| A | HIS220 |
| A | PHE232 |
| A | GLY235 |
| A | ASP237 |
| A | THR345 |
| A | MET346 |
| A | GLY347 |
| A | PHE348 |
| A | GLY383 |
| A | GLN384 |
| A | GLY693 |
| A | ARG694 |
| A | VAL695 |
| A | LEU696 |
| A | HIS698 |
| A | TRP699 |
| A | HIS700 |
| A | LYS793 |
| A | LYS794 |
| A | MO1802 |
| A | MGD1803 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEC B1128 |
| Chain | Residue |
| B | ARG30 |
| B | PRO40 |
| B | VAL41 |
| B | ILE42 |
| B | PRO43 |
| B | HIS44 |
| B | TYR49 |
| B | ARG57 |
| B | CYS58 |
| B | CYS61 |
| B | HIS62 |
| B | CYS98 |
| B | HIS102 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC B1129 |
| Chain | Residue |
| B | PHE97 |
| B | CYS98 |
| B | CYS101 |
| B | HIS102 |
| F | ARG64 |
| F | ILE77 |
| A | LEU52 |
| A | ASN53 |
| A | TYR58 |
| B | ARG33 |
| B | TYR35 |
| B | PRO36 |
| B | GLU37 |
| B | GLN38 |
| B | PRO40 |
| B | HIS62 |
| B | MET74 |
| B | ILE75 |
| B | HIS79 |
| B | ARG95 |
| B | TYR96 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 C1801 |
| Chain | Residue |
| C | CYS19 |
| C | CYS22 |
| C | CYS26 |
| C | ASN53 |
| C | CYS54 |
| C | GLY57 |
| C | PRO194 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO C1802 |
| Chain | Residue |
| C | CYS152 |
| C | MGD1803 |
| C | MGD1804 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE MGD C1803 |
| Chain | Residue |
| C | ARG20 |
| C | GLN123 |
| C | ASN148 |
| C | CYS152 |
| C | MET346 |
| C | GLN350 |
| C | GLN384 |
| C | VAL454 |
| C | ASN455 |
| C | ASN456 |
| C | ASN457 |
| C | ALA460 |
| C | SER482 |
| C | ASP483 |
| C | THR487 |
| C | ALA499 |
| C | ALA500 |
| C | MET501 |
| C | LYS505 |
| C | ASP532 |
| C | THR692 |
| C | ARG694 |
| C | TRP699 |
| C | HIS700 |
| C | SER701 |
| C | SER703 |
| C | TRP768 |
| C | ASN776 |
| C | PHE792 |
| C | LYS793 |
| C | MO1802 |
| C | MGD1804 |
| site_id | BC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE MGD C1804 |
| Chain | Residue |
| C | LYS56 |
| C | CYS152 |
| C | TRP185 |
| C | GLY186 |
| C | ASN188 |
| C | GLU191 |
| C | MET192 |
| C | SER216 |
| C | THR217 |
| C | HIS220 |
| C | PHE232 |
| C | GLY235 |
| C | ASP237 |
| C | THR345 |
| C | MET346 |
| C | GLY347 |
| C | PHE348 |
| C | GLY383 |
| C | GLN384 |
| C | GLY693 |
| C | ARG694 |
| C | VAL695 |
| C | LEU696 |
| C | HIS698 |
| C | TRP699 |
| C | HIS700 |
| C | LYS793 |
| C | LYS794 |
| C | MO1802 |
| C | MGD1803 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEC D1128 |
| Chain | Residue |
| D | ARG30 |
| D | PRO40 |
| D | VAL41 |
| D | ILE42 |
| D | PRO43 |
| D | HIS44 |
| D | TYR49 |
| D | CYS58 |
| D | CYS61 |
| D | HIS62 |
| D | CYS98 |
| D | HEC1129 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC D1129 |
| Chain | Residue |
| C | LEU52 |
| C | ASN53 |
| C | TYR58 |
| D | ARG33 |
| D | TYR35 |
| D | PRO36 |
| D | GLU37 |
| D | GLN38 |
| D | PRO40 |
| D | HIS62 |
| D | MET74 |
| D | ILE75 |
| D | HIS79 |
| D | ARG95 |
| D | PHE97 |
| D | CYS98 |
| D | CYS101 |
| D | HIS102 |
| D | HEC1128 |
| H | ARG64 |
| H | ILE77 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 E1801 |
| Chain | Residue |
| E | CYS19 |
| E | CYS22 |
| E | CYS26 |
| E | CYS54 |
| E | GLY57 |
| E | PRO194 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO E1802 |
| Chain | Residue |
| E | CYS152 |
| E | MGD1803 |
| E | MGD1804 |
| site_id | BC6 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD E1803 |
| Chain | Residue |
| E | ARG20 |
| E | GLN123 |
| E | ASN148 |
| E | CYS152 |
| E | MET346 |
| E | GLN350 |
| E | GLN384 |
| E | VAL454 |
| E | ASN455 |
| E | ASN456 |
| E | ALA460 |
| E | SER482 |
| E | ASP483 |
| E | THR487 |
| E | ALA499 |
| E | ALA500 |
| E | MET501 |
| E | LYS505 |
| E | ASP532 |
| E | THR692 |
| E | ARG694 |
| E | TRP699 |
| E | HIS700 |
| E | SER701 |
| E | SER703 |
| E | TRP768 |
| E | ASN776 |
| E | PHE792 |
| E | LYS793 |
| E | MO1802 |
| E | MGD1804 |
| site_id | BC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE MGD E1804 |
| Chain | Residue |
| E | LYS56 |
| E | CYS152 |
| E | TRP185 |
| E | GLY186 |
| E | ASN188 |
| E | GLU191 |
| E | MET192 |
| E | SER216 |
| E | THR217 |
| E | HIS220 |
| E | PHE232 |
| E | GLY235 |
| E | ASP237 |
| E | THR345 |
| E | MET346 |
| E | GLY347 |
| E | PHE348 |
| E | GLY383 |
| E | GLN384 |
| E | GLY693 |
| E | ARG694 |
| E | VAL695 |
| E | LEU696 |
| E | HIS698 |
| E | TRP699 |
| E | HIS700 |
| E | LYS793 |
| E | LYS794 |
| E | MO1802 |
| E | MGD1803 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEC F1128 |
| Chain | Residue |
| F | ARG30 |
| F | VAL41 |
| F | ILE42 |
| F | PRO43 |
| F | HIS44 |
| F | TYR49 |
| F | ARG57 |
| F | CYS58 |
| F | CYS61 |
| F | HIS62 |
| F | HEC1129 |
| site_id | BC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC F1129 |
| Chain | Residue |
| B | ARG64 |
| B | TYR66 |
| B | ILE77 |
| E | LEU52 |
| E | ASN53 |
| E | TYR58 |
| F | ARG33 |
| F | TYR35 |
| F | PRO36 |
| F | GLU37 |
| F | GLN38 |
| F | PRO40 |
| F | HIS62 |
| F | MET74 |
| F | ILE75 |
| F | HIS79 |
| F | ARG95 |
| F | PHE97 |
| F | CYS98 |
| F | CYS101 |
| F | HIS102 |
| F | HEC1128 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 G1801 |
| Chain | Residue |
| G | CYS19 |
| G | CYS22 |
| G | CYS26 |
| G | CYS54 |
| G | PRO194 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO G1802 |
| Chain | Residue |
| G | CYS152 |
| G | MGD1803 |
| G | MGD1804 |
| site_id | CC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE MGD G1803 |
| Chain | Residue |
| G | ARG20 |
| G | GLN123 |
| G | ASN148 |
| G | CYS152 |
| G | MET346 |
| G | GLN350 |
| G | GLN384 |
| G | VAL454 |
| G | ASN455 |
| G | ASN456 |
| G | ASN457 |
| G | ALA460 |
| G | SER482 |
| G | ASP483 |
| G | THR487 |
| G | ALA499 |
| G | ALA500 |
| G | MET501 |
| G | LYS505 |
| G | ASP532 |
| G | THR692 |
| G | ARG694 |
| G | TRP699 |
| G | HIS700 |
| G | SER701 |
| G | SER703 |
| G | TRP768 |
| G | ASN776 |
| G | PHE792 |
| G | LYS793 |
| G | MO1802 |
| G | MGD1804 |
| site_id | CC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE MGD G1804 |
| Chain | Residue |
| G | LYS56 |
| G | CYS152 |
| G | TRP185 |
| G | GLY186 |
| G | SER187 |
| G | ASN188 |
| G | GLU191 |
| G | MET192 |
| G | SER216 |
| G | THR217 |
| G | HIS220 |
| G | GLY235 |
| G | ASP237 |
| G | THR345 |
| G | MET346 |
| G | GLY347 |
| G | PHE348 |
| G | GLY383 |
| G | GLN384 |
| G | GLY693 |
| G | ARG694 |
| G | VAL695 |
| G | LEU696 |
| G | HIS698 |
| G | TRP699 |
| G | HIS700 |
| G | LYS793 |
| G | LYS794 |
| G | MO1802 |
| G | MGD1803 |
| site_id | CC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC H1128 |
| Chain | Residue |
| H | ARG30 |
| H | ARG33 |
| H | PRO40 |
| H | VAL41 |
| H | ILE42 |
| H | PRO43 |
| H | HIS44 |
| H | TYR49 |
| H | ARG57 |
| H | CYS58 |
| H | CYS61 |
| H | HIS62 |
| H | HIS102 |
| H | HEC1129 |
| site_id | CC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC H1129 |
| Chain | Residue |
| D | ARG64 |
| D | TYR66 |
| D | ILE77 |
| G | LEU52 |
| G | ASN53 |
| G | TYR58 |
| H | ARG33 |
| H | TYR35 |
| H | PRO36 |
| H | GLU37 |
| H | GLN38 |
| H | PRO40 |
| H | HIS62 |
| H | MET74 |
| H | ILE75 |
| H | HIS79 |
| H | ARG95 |
| H | CYS98 |
| H | CYS101 |
| H | HIS102 |
| H | HEC1128 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 I1801 |
| Chain | Residue |
| I | CYS19 |
| I | PHE21 |
| I | CYS22 |
| I | GLY25 |
| I | CYS26 |
| I | CYS54 |
| I | PRO194 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO I1802 |
| Chain | Residue |
| I | CYS152 |
| I | MGD1803 |
| I | MGD1804 |
| site_id | CC9 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE MGD I1803 |
| Chain | Residue |
| I | ARG20 |
| I | GLN123 |
| I | ASN148 |
| I | CYS152 |
| I | MET346 |
| I | GLN350 |
| I | GLN384 |
| I | VAL454 |
| I | ASN455 |
| I | ASN456 |
| I | ASN457 |
| I | ALA460 |
| I | SER482 |
| I | ASP483 |
| I | THR487 |
| I | ALA499 |
| I | ALA500 |
| I | MET501 |
| I | LYS505 |
| I | ASP532 |
| I | THR692 |
| I | ARG694 |
| I | TRP699 |
| I | HIS700 |
| I | SER701 |
| I | SER703 |
| I | TRP768 |
| I | ASN776 |
| I | PHE792 |
| I | LYS793 |
| I | MO1802 |
| I | MGD1804 |
| site_id | DC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD I1804 |
| Chain | Residue |
| I | LYS56 |
| I | CYS152 |
| I | TRP185 |
| I | GLY186 |
| I | SER187 |
| I | ASN188 |
| I | GLU191 |
| I | MET192 |
| I | SER216 |
| I | THR217 |
| I | HIS220 |
| I | PHE232 |
| I | GLY235 |
| I | ASP237 |
| I | THR345 |
| I | MET346 |
| I | GLY347 |
| I | PHE348 |
| I | GLY383 |
| I | GLN384 |
| I | GLY693 |
| I | ARG694 |
| I | VAL695 |
| I | LEU696 |
| I | HIS698 |
| I | TRP699 |
| I | HIS700 |
| I | LYS793 |
| I | LYS794 |
| I | MO1802 |
| I | MGD1803 |
| site_id | DC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEC J1128 |
| Chain | Residue |
| J | ARG30 |
| J | ARG33 |
| J | PRO40 |
| J | VAL41 |
| J | ILE42 |
| J | PRO43 |
| J | HIS44 |
| J | TYR49 |
| J | ARG57 |
| J | CYS58 |
| J | CYS61 |
| J | HIS62 |
| J | HEC1129 |
| site_id | DC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC J1129 |
| Chain | Residue |
| I | LEU52 |
| I | TYR58 |
| J | ARG33 |
| J | TYR35 |
| J | PRO36 |
| J | GLU37 |
| J | GLN38 |
| J | PRO40 |
| J | LEU59 |
| J | HIS62 |
| J | MET74 |
| J | ILE75 |
| J | SER76 |
| J | HIS79 |
| J | ARG95 |
| J | PHE97 |
| J | CYS98 |
| J | CYS101 |
| J | HIS102 |
| J | HEC1128 |
| P | ARG64 |
| P | TYR66 |
| P | ILE77 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 K1801 |
| Chain | Residue |
| K | CYS19 |
| K | CYS22 |
| K | CYS26 |
| K | CYS54 |
| K | GLY57 |
| K | PRO194 |
| site_id | DC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO K1802 |
| Chain | Residue |
| K | CYS152 |
| K | MGD1803 |
| K | MGD1804 |
| site_id | DC6 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD K1803 |
| Chain | Residue |
| K | ARG20 |
| K | GLN123 |
| K | ASN148 |
| K | CYS152 |
| K | GLN350 |
| K | GLN384 |
| K | VAL454 |
| K | ASN455 |
| K | ASN456 |
| K | ASN457 |
| K | ALA460 |
| K | SER482 |
| K | ASP483 |
| K | THR487 |
| K | ALA499 |
| K | ALA500 |
| K | MET501 |
| K | LYS505 |
| K | ASP532 |
| K | THR692 |
| K | ARG694 |
| K | TRP699 |
| K | HIS700 |
| K | SER701 |
| K | SER703 |
| K | TRP768 |
| K | ASN776 |
| K | PHE792 |
| K | LYS793 |
| K | MO1802 |
| K | MGD1804 |
| site_id | DC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD K1804 |
| Chain | Residue |
| K | LYS56 |
| K | CYS152 |
| K | TRP185 |
| K | GLY186 |
| K | SER187 |
| K | ASN188 |
| K | GLU191 |
| K | MET192 |
| K | SER216 |
| K | THR217 |
| K | HIS220 |
| K | PHE232 |
| K | GLY235 |
| K | ASP237 |
| K | THR345 |
| K | MET346 |
| K | GLY347 |
| K | PHE348 |
| K | GLY383 |
| K | GLN384 |
| K | GLY693 |
| K | ARG694 |
| K | VAL695 |
| K | LEU696 |
| K | HIS698 |
| K | TRP699 |
| K | HIS700 |
| K | LYS793 |
| K | LYS794 |
| K | MO1802 |
| K | MGD1803 |
| site_id | DC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC L1128 |
| Chain | Residue |
| L | ARG30 |
| L | ARG33 |
| L | PRO40 |
| L | VAL41 |
| L | ILE42 |
| L | PRO43 |
| L | HIS44 |
| L | TYR49 |
| L | ARG57 |
| L | CYS58 |
| L | CYS61 |
| L | HIS62 |
| L | HIS102 |
| L | HEC1129 |
| site_id | DC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC L1129 |
| Chain | Residue |
| K | LEU52 |
| K | ASN53 |
| K | TYR58 |
| L | ARG33 |
| L | TYR35 |
| L | PRO36 |
| L | GLU37 |
| L | GLN38 |
| L | PRO40 |
| L | HIS62 |
| L | MET74 |
| L | ILE75 |
| L | HIS79 |
| L | ARG95 |
| L | PHE97 |
| L | CYS98 |
| L | CYS101 |
| L | HIS102 |
| L | HEC1128 |
| N | ARG64 |
| N | TYR66 |
| N | ILE77 |
| site_id | EC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 M1801 |
| Chain | Residue |
| M | CYS19 |
| M | CYS22 |
| M | CYS26 |
| M | CYS54 |
| M | GLY57 |
| M | PRO194 |
| site_id | EC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO M1802 |
| Chain | Residue |
| M | CYS152 |
| M | MGD1803 |
| M | MGD1804 |
| site_id | EC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE MGD M1803 |
| Chain | Residue |
| M | ARG20 |
| M | GLN123 |
| M | ASN148 |
| M | CYS152 |
| M | MET346 |
| M | GLN350 |
| M | GLN384 |
| M | VAL454 |
| M | ASN455 |
| M | ASN456 |
| M | ASN457 |
| M | ALA460 |
| M | SER482 |
| M | ASP483 |
| M | THR487 |
| M | ALA499 |
| M | ALA500 |
| M | MET501 |
| M | LYS505 |
| M | ASP532 |
| M | THR692 |
| M | ARG694 |
| M | TRP699 |
| M | HIS700 |
| M | SER701 |
| M | SER703 |
| M | TRP768 |
| M | ASN776 |
| M | PHE792 |
| M | LYS793 |
| M | MO1802 |
| M | MGD1804 |
| site_id | EC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD M1804 |
| Chain | Residue |
| M | LYS56 |
| M | CYS152 |
| M | TRP185 |
| M | GLY186 |
| M | SER187 |
| M | ASN188 |
| M | GLU191 |
| M | MET192 |
| M | SER216 |
| M | THR217 |
| M | HIS220 |
| M | PHE232 |
| M | GLY235 |
| M | ASP237 |
| M | THR345 |
| M | MET346 |
| M | GLY347 |
| M | PHE348 |
| M | GLY383 |
| M | GLN384 |
| M | GLY693 |
| M | ARG694 |
| M | VAL695 |
| M | LEU696 |
| M | HIS698 |
| M | TRP699 |
| M | HIS700 |
| M | LYS793 |
| M | LYS794 |
| M | MO1802 |
| M | MGD1803 |
| site_id | EC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC N1128 |
| Chain | Residue |
| N | ARG30 |
| N | ARG33 |
| N | PRO40 |
| N | VAL41 |
| N | ILE42 |
| N | PRO43 |
| N | HIS44 |
| N | TYR49 |
| N | ARG57 |
| N | CYS58 |
| N | CYS61 |
| N | HIS62 |
| N | HIS102 |
| N | HEC1129 |
| site_id | EC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC N1129 |
| Chain | Residue |
| L | ARG64 |
| L | ILE77 |
| M | LEU52 |
| M | ASN53 |
| M | TYR58 |
| N | ARG33 |
| N | PRO36 |
| N | GLU37 |
| N | GLN38 |
| N | PRO40 |
| N | HIS62 |
| N | MET74 |
| N | ILE75 |
| N | HIS79 |
| N | ARG95 |
| N | PHE97 |
| N | CYS98 |
| N | CYS101 |
| N | HIS102 |
| N | HEC1128 |
| site_id | EC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 O1801 |
| Chain | Residue |
| O | CYS19 |
| O | CYS22 |
| O | CYS26 |
| O | ASN53 |
| O | CYS54 |
| O | GLY57 |
| O | PRO194 |
| site_id | EC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MO O1802 |
| Chain | Residue |
| O | CYS152 |
| O | MGD1803 |
| O | MGD1804 |
| site_id | EC9 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE MGD O1803 |
| Chain | Residue |
| O | ARG20 |
| O | GLN123 |
| O | ASN148 |
| O | CYS152 |
| O | MET346 |
| O | GLN350 |
| O | GLN384 |
| O | VAL454 |
| O | ASN455 |
| O | ASN456 |
| O | ASN457 |
| O | ALA460 |
| O | SER482 |
| O | ASP483 |
| O | THR487 |
| O | ALA499 |
| O | ALA500 |
| O | MET501 |
| O | LYS505 |
| O | ASP532 |
| O | THR692 |
| O | ARG694 |
| O | TRP699 |
| O | HIS700 |
| O | SER701 |
| O | SER703 |
| O | TRP768 |
| O | ASN776 |
| O | PHE792 |
| O | LYS793 |
| O | MO1802 |
| O | MGD1804 |
| site_id | FC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE MGD O1804 |
| Chain | Residue |
| O | LYS56 |
| O | CYS152 |
| O | TRP185 |
| O | GLY186 |
| O | SER187 |
| O | ASN188 |
| O | GLU191 |
| O | MET192 |
| O | SER216 |
| O | THR217 |
| O | HIS220 |
| O | PHE232 |
| O | GLY235 |
| O | ASP237 |
| O | THR345 |
| O | MET346 |
| O | GLY347 |
| O | PHE348 |
| O | GLY383 |
| O | GLN384 |
| O | GLY693 |
| O | ARG694 |
| O | VAL695 |
| O | LEU696 |
| O | HIS698 |
| O | TRP699 |
| O | HIS700 |
| O | LYS793 |
| O | LYS794 |
| O | MO1802 |
| O | MGD1803 |
| site_id | FC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC P1128 |
| Chain | Residue |
| P | ARG30 |
| P | ARG33 |
| P | VAL41 |
| P | ILE42 |
| P | PRO43 |
| P | HIS44 |
| P | TYR49 |
| P | ARG57 |
| P | CYS58 |
| P | CYS61 |
| P | HIS62 |
| P | CYS98 |
| P | HIS102 |
| P | HEC1129 |
| site_id | FC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC P1129 |
| Chain | Residue |
| J | ARG64 |
| J | TYR66 |
| J | ILE77 |
| O | LEU52 |
| O | ASN53 |
| O | TYR58 |
| P | ARG33 |
| P | TYR35 |
| P | PRO36 |
| P | GLU37 |
| P | GLN38 |
| P | PRO40 |
| P | HIS62 |
| P | MET74 |
| P | ILE75 |
| P | HIS79 |
| P | ARG95 |
| P | PHE97 |
| P | CYS98 |
| P | CYS101 |
| P | HIS102 |
| P | HEC1128 |
Functional Information from PROSITE/UniProt
| site_id | PS00551 |
| Number of Residues | 18 |
| Details | MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. ApCrf.CGTgCgVmVgtr.D |
| Chain | Residue | Details |
| A | ALA17-ASP34 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| B | HIS44 | |
| F | HIS62 | |
| K | LYS56 | |
| K | GLN123 | |
| K | ASN148 | |
| K | CYS152 | |
| K | TRP185 | |
| K | GLY235 | |
| K | MET346 | |
| K | GLN350 | |
| K | ASN456 | |
| K | SER482 | |
| F | HIS79 | |
| K | LYS505 | |
| K | ASP532 | |
| K | THR692 | |
| K | ASN776 | |
| K | LYS793 | |
| M | CYS19 | |
| M | CYS22 | |
| M | CYS26 | |
| M | CYS54 | |
| M | LYS56 | |
| F | HIS102 | |
| M | GLN123 | |
| M | ASN148 | |
| M | CYS152 | |
| M | TRP185 | |
| M | GLY235 | |
| M | MET346 | |
| M | GLN350 | |
| M | ASN456 | |
| M | SER482 | |
| M | LYS505 | |
| H | HIS44 | |
| M | ASP532 | |
| M | THR692 | |
| M | ASN776 | |
| M | LYS793 | |
| O | CYS19 | |
| O | CYS22 | |
| O | CYS26 | |
| O | CYS54 | |
| O | LYS56 | |
| O | GLN123 | |
| H | HIS62 | |
| O | ASN148 | |
| O | CYS152 | |
| O | TRP185 | |
| O | GLY235 | |
| O | MET346 | |
| O | GLN350 | |
| O | ASN456 | |
| O | SER482 | |
| O | LYS505 | |
| O | ASP532 | |
| H | HIS79 | |
| O | THR692 | |
| O | ASN776 | |
| O | LYS793 | |
| H | HIS102 | |
| J | HIS44 | |
| J | HIS62 | |
| J | HIS79 | |
| B | HIS62 | |
| J | HIS102 | |
| L | HIS44 | |
| L | HIS62 | |
| L | HIS79 | |
| L | HIS102 | |
| N | HIS44 | |
| N | HIS62 | |
| N | HIS79 | |
| N | HIS102 | |
| P | HIS44 | |
| B | HIS79 | |
| P | HIS62 | |
| P | HIS79 | |
| P | HIS102 | |
| C | SER482 | |
| C | LYS505 | |
| C | ASP532 | |
| C | THR692 | |
| C | ASN776 | |
| C | LYS793 | |
| E | CYS19 | |
| B | HIS102 | |
| E | CYS22 | |
| E | CYS26 | |
| E | CYS54 | |
| E | LYS56 | |
| E | GLN123 | |
| E | ASN148 | |
| E | CYS152 | |
| E | TRP185 | |
| E | GLY235 | |
| E | MET346 | |
| D | HIS44 | |
| E | GLN350 | |
| E | ASN456 | |
| E | SER482 | |
| E | LYS505 | |
| E | ASP532 | |
| E | THR692 | |
| E | ASN776 | |
| E | LYS793 | |
| G | CYS19 | |
| G | CYS22 | |
| D | HIS62 | |
| G | CYS26 | |
| G | CYS54 | |
| G | LYS56 | |
| G | GLN123 | |
| G | ASN148 | |
| G | CYS152 | |
| G | TRP185 | |
| G | GLY235 | |
| G | MET346 | |
| G | GLN350 | |
| D | HIS79 | |
| G | ASN456 | |
| G | SER482 | |
| G | LYS505 | |
| G | ASP532 | |
| G | THR692 | |
| G | ASN776 | |
| G | LYS793 | |
| I | CYS19 | |
| I | CYS22 | |
| I | CYS26 | |
| D | HIS102 | |
| I | CYS54 | |
| I | LYS56 | |
| I | GLN123 | |
| I | ASN148 | |
| I | CYS152 | |
| I | TRP185 | |
| I | GLY235 | |
| I | MET346 | |
| I | GLN350 | |
| I | ASN456 | |
| F | HIS44 | |
| I | SER482 | |
| I | LYS505 | |
| I | ASP532 | |
| I | THR692 | |
| I | ASN776 | |
| I | LYS793 | |
| K | CYS19 | |
| K | CYS22 | |
| K | CYS26 | |
| K | CYS54 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: covalent => ECO:0000269|PubMed:14528294 |
| Chain | Residue | Details |
| B | CYS58 | |
| F | CYS61 | |
| F | CYS98 | |
| F | CYS101 | |
| H | CYS58 | |
| H | CYS61 | |
| H | CYS98 | |
| H | CYS101 | |
| J | CYS58 | |
| J | CYS61 | |
| J | CYS98 | |
| B | CYS61 | |
| J | CYS101 | |
| L | CYS58 | |
| L | CYS61 | |
| L | CYS98 | |
| L | CYS101 | |
| N | CYS58 | |
| N | CYS61 | |
| N | CYS98 | |
| N | CYS101 | |
| P | CYS58 | |
| B | CYS98 | |
| P | CYS61 | |
| P | CYS98 | |
| P | CYS101 | |
| B | CYS101 | |
| D | CYS58 | |
| D | CYS61 | |
| D | CYS98 | |
| D | CYS101 | |
| F | CYS58 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000255 |
| Chain | Residue | Details |
| B | GLN1 | |
| D | GLN1 | |
| F | GLN1 | |
| H | GLN1 | |
| J | GLN1 | |
| L | GLN1 | |
| N | GLN1 | |
| P | GLN1 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| A | CYS152 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| C | CYS152 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| E | CYS152 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| G | CYS152 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| I | CYS152 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| K | CYS152 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| M | CYS152 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| O | CYS152 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| A | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| A | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| A | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| A | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| A | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| C | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| C | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| C | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| C | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| C | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| E | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| E | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| E | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| E | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| E | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| E | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| G | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| G | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| G | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| G | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| G | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| G | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| I | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| I | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| I | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| I | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| I | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| I | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| K | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| K | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| K | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| K | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| K | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| K | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA7 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| M | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| M | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| M | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| M | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| M | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| M | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA8 |
| Number of Residues | 6 |
| Details | M-CSA 276 |
| Chain | Residue | Details |
| O | LYS56 | activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| O | CYS152 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile |
| O | MET153 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| O | MET346 | electrostatic stabiliser, polar/non-polar interaction, steric role |
| O | GLY383 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| O | GLN384 | electrostatic stabiliser, hydrogen bond acceptor |
