Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0070225 | molecular_function | sulfide dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0070225 | molecular_function | sulfide dehydrogenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 699 |
| Chain | Residue |
| A | VAL8 |
| A | TYR43 |
| A | ASN46 |
| A | ALA77 |
| A | ALA103 |
| A | PRO104 |
| A | GLY105 |
| A | TRP128 |
| A | ARG160 |
| A | CYS161 |
| A | ILE261 |
| A | GLY9 |
| A | GLY293 |
| A | ASP294 |
| A | SER304 |
| A | GLY305 |
| A | TYR306 |
| A | TYR338 |
| A | TRP391 |
| A | GLY11 |
| A | GLY13 |
| A | ILE33 |
| A | GLU34 |
| A | PRO35 |
| A | TYR39 |
| A | CYS42 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC C 901 |
| Chain | Residue |
| A | TYR306 |
| A | THR336 |
| A | TYR338 |
| A | TYR387 |
| C | CYS11 |
| C | CYS14 |
| C | HIS15 |
| C | PRO27 |
| C | ILE29 |
| C | PHE37 |
| C | MET41 |
| C | PHE44 |
| C | SER51 |
| C | THR52 |
| C | ILE53 |
| C | MET54 |
| C | TYR61 |
| C | TYR128 |
| C | HEC902 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEC C 902 |
| Chain | Residue |
| C | TYR100 |
| C | CYS101 |
| C | CYS104 |
| C | HIS105 |
| C | HIS119 |
| C | TYR128 |
| C | ARG141 |
| C | PRO142 |
| C | GLU144 |
| C | MET147 |
| C | LEU155 |
| C | LEU166 |
| C | HEC901 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD B 699 |
| Chain | Residue |
| B | VAL8 |
| B | GLY9 |
| B | GLY11 |
| B | THR12 |
| B | GLY13 |
| B | ILE33 |
| B | GLU34 |
| B | PRO35 |
| B | TYR39 |
| B | CYS42 |
| B | TYR43 |
| B | ASN46 |
| B | ALA77 |
| B | ALA103 |
| B | PRO104 |
| B | GLY105 |
| B | ARG160 |
| B | CYS161 |
| B | GLY293 |
| B | ASP294 |
| B | LYS303 |
| B | SER304 |
| B | GLY305 |
| B | TYR306 |
| B | TYR338 |
| B | TRP391 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC D 901 |
| Chain | Residue |
| D | MET54 |
| D | ILE57 |
| D | TYR61 |
| D | TYR128 |
| D | HEC902 |
| B | TYR306 |
| B | LEU334 |
| B | THR336 |
| B | TYR387 |
| D | CYS11 |
| D | CYS14 |
| D | HIS15 |
| D | ILE29 |
| D | MET32 |
| D | PHE37 |
| D | MET41 |
| D | PHE44 |
| D | SER51 |
| D | THR52 |
| D | ILE53 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEC D 902 |
| Chain | Residue |
| D | TYR100 |
| D | CYS101 |
| D | LYS103 |
| D | CYS104 |
| D | HIS105 |
| D | HIS119 |
| D | TYR128 |
| D | MET133 |
| D | PHE136 |
| D | ARG141 |
| D | PRO142 |
| D | GLU144 |
| D | LYS146 |
| D | MET147 |
| D | HEC901 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: covalent |
| Chain | Residue | Details |
| C | CYS11 | |
| C | CYS14 | |
| C | CYS101 | |
| C | CYS104 | |
| D | CYS11 | |
| D | CYS14 | |
| D | CYS101 | |
| D | CYS104 | |
| Chain | Residue | Details |
| C | HIS15 | |
| C | MET54 | |
| C | HIS105 | |
| C | MET143 | |
| D | HIS15 | |
| D | MET54 | |
| D | HIS105 | |
| D | MET143 | |
