Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0042597 | cellular_component | periplasmic space |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 601 |
| Chain | Residue |
| A | PHE53 |
| A | ILE162 |
| A | ASN333 |
| A | ILE369 |
| A | LEU433 |
| A | HEM602 |
| A | HOH2164 |
| A | HOH2348 |
| A | HOH2349 |
| A | HOH2350 |
| A | HOH2351 |
| A | ASP54 |
| A | HOH2352 |
| A | SER58 |
| A | HIS59 |
| A | LEU60 |
| A | CYS79 |
| A | CYS82 |
| A | HIS83 |
| A | PHE85 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM A 602 |
| Chain | Residue |
| A | HIS40 |
| A | TYR43 |
| A | LEU46 |
| A | PRO55 |
| A | HIS56 |
| A | CYS65 |
| A | CYS68 |
| A | HIS69 |
| A | LYS88 |
| A | MET90 |
| A | HEM601 |
| A | HEM603 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 603 |
| Chain | Residue |
| A | MET5 |
| A | HIS9 |
| A | SER17 |
| A | GLN35 |
| A | CYS36 |
| A | CYS39 |
| A | HIS40 |
| A | HIS69 |
| A | PRO91 |
| A | ASP227 |
| A | HEM602 |
| A | HEM604 |
| A | HOH2354 |
| A | HOH2355 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 604 |
| Chain | Residue |
| A | GLY6 |
| A | HIS9 |
| A | CYS15 |
| A | CYS18 |
| A | HIS19 |
| A | GLU29 |
| A | THR66 |
| A | LYS70 |
| A | GLY71 |
| A | HIS72 |
| A | HIS293 |
| A | VAL467 |
| A | ALA468 |
| A | SER469 |
| A | GLY470 |
| A | HEM603 |
| A | HOH2072 |
| A | HOH2356 |
| site_id | AC5 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE FAD A 605 |
| Chain | Residue |
| A | HOH2110 |
| A | HOH2189 |
| A | HOH2191 |
| A | HOH2216 |
| A | HOH2339 |
| A | HOH2357 |
| A | HOH2358 |
| A | VAL127 |
| A | GLY128 |
| A | GLY130 |
| A | SER131 |
| A | ALA132 |
| A | ASP151 |
| A | LYS152 |
| A | GLY157 |
| A | GLY158 |
| A | ASN159 |
| A | SER160 |
| A | SER163 |
| A | ALA164 |
| A | GLY165 |
| A | GLY166 |
| A | SER271 |
| A | ARG272 |
| A | VAL273 |
| A | ALA307 |
| A | THR308 |
| A | GLY309 |
| A | SER331 |
| A | ASN332 |
| A | THR335 |
| A | ASP339 |
| A | HIS499 |
| A | HIS500 |
| A | GLY528 |
| A | GLU529 |
| A | ARG539 |
| A | GLY542 |
| A | ASN543 |
| A | ALA544 |
| A | ILE545 |
| A | THR548 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM D 601 |
| Chain | Residue |
| D | ASP54 |
| D | SER58 |
| D | HIS59 |
| D | LEU60 |
| D | CYS79 |
| D | CYS82 |
| D | HIS83 |
| D | PHE85 |
| D | ILE162 |
| D | ASN333 |
| D | ILE369 |
| D | LEU433 |
| D | HEM602 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM D 602 |
| Chain | Residue |
| D | HIS40 |
| D | TYR43 |
| D | LEU46 |
| D | PRO55 |
| D | HIS56 |
| D | CYS65 |
| D | CYS68 |
| D | HIS69 |
| D | PHE77 |
| D | LYS88 |
| D | MET90 |
| D | LYS193 |
| D | HEM601 |
| D | HEM603 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEM D 603 |
| Chain | Residue |
| D | MET5 |
| D | HIS9 |
| D | SER17 |
| D | CYS36 |
| D | CYS39 |
| D | HIS40 |
| D | HIS69 |
| D | PRO91 |
| D | PHE92 |
| D | LYS193 |
| D | HEM602 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM D 604 |
| Chain | Residue |
| D | MET5 |
| D | GLY6 |
| D | HIS9 |
| D | CYS15 |
| D | CYS18 |
| D | HIS19 |
| D | ILE23 |
| D | VAL25 |
| D | THR66 |
| D | LYS70 |
| D | GLY71 |
| D | HIS72 |
| D | GLU73 |
| D | HIS293 |
| D | HOH2146 |
| site_id | BC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD D 605 |
| Chain | Residue |
| D | VAL127 |
| D | GLY128 |
| D | GLY130 |
| D | SER131 |
| D | ALA132 |
| D | ASP151 |
| D | LYS152 |
| D | GLY157 |
| D | GLY158 |
| D | ASN159 |
| D | SER160 |
| D | SER163 |
| D | ALA164 |
| D | GLY165 |
| D | SER271 |
| D | ARG272 |
| D | VAL273 |
| D | ALA307 |
| D | THR308 |
| D | GLY309 |
| D | SER331 |
| D | ASN332 |
| D | THR335 |
| D | ASP339 |
| D | HIS499 |
| D | HIS500 |
| D | GLY528 |
| D | GLU529 |
| D | ARG539 |
| D | GLY542 |
| D | ASN543 |
| D | ALA544 |
| D | ILE545 |
| D | THR548 |
| D | HOH2132 |
| D | HOH2134 |
| D | HOH2147 |
| D | HOH2148 |
| D | HOH2149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0C278","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10581549","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QO8","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10581549","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QO8","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d4c |
| Chain | Residue | Details |
| A | HIS360 | |
| A | HIS499 | |
| A | ARG397 | |
| A | ARG539 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d4c |
| Chain | Residue | Details |
| D | HIS360 | |
| D | HIS499 | |
| D | ARG397 | |
| D | ARG539 | |