Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009061 | biological_process | anaerobic respiration |
| 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 | 0019645 | biological_process | anaerobic electron transport chain |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0019645 | biological_process | anaerobic electron transport chain |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1810 |
| Chain | Residue |
| A | THR506 |
| A | MET507 |
| A | GLY508 |
| A | GLU534 |
| A | THR536 |
| A | HOH1837 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 2810 |
| Chain | Residue |
| B | GLU534 |
| B | THR536 |
| B | HOH1036 |
| B | THR506 |
| B | MET507 |
| B | GLY508 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM A 801 |
| Chain | Residue |
| A | HIS8 |
| A | VAL9 |
| A | CYS14 |
| A | CYS17 |
| A | HIS18 |
| A | LEU24 |
| A | SER73 |
| A | ALA74 |
| A | HIS75 |
| A | HEM802 |
| A | HOH1866 |
| A | HOH2015 |
| A | HOH2112 |
| A | HOH2334 |
| A | HOH2607 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 802 |
| Chain | Residue |
| A | LEU4 |
| A | PHE7 |
| A | HIS8 |
| A | GLN12 |
| A | SER16 |
| A | CYS36 |
| A | CYS39 |
| A | HIS40 |
| A | HIS72 |
| A | TYR94 |
| A | HEM801 |
| A | HEM803 |
| A | HOH1948 |
| A | HOH2274 |
| A | HOH2370 |
| A | HOH2438 |
| A | HOH2480 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 803 |
| Chain | Residue |
| A | HIS40 |
| A | LEU43 |
| A | VAL46 |
| A | THR49 |
| A | THR50 |
| A | HIS52 |
| A | ALA57 |
| A | HIS58 |
| A | VAL66 |
| A | ALA67 |
| A | CYS68 |
| A | CYS71 |
| A | HIS72 |
| A | PHE90 |
| A | ASN91 |
| A | MET92 |
| A | HEM802 |
| A | HEM804 |
| A | HOH1823 |
| A | HOH2110 |
| A | HOH2155 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 804 |
| Chain | Residue |
| A | HIS54 |
| A | TYR55 |
| A | ASN56 |
| A | SER60 |
| A | HIS61 |
| A | PHE62 |
| A | CYS82 |
| A | SER84 |
| A | CYS85 |
| A | HIS86 |
| A | PHE88 |
| A | LEU167 |
| A | VAL374 |
| A | LYS431 |
| A | LYS434 |
| A | TYR435 |
| A | HEM803 |
| A | HOH1899 |
| A | HOH1908 |
| A | HOH1921 |
| A | HOH1926 |
| A | HOH1931 |
| A | HOH2010 |
| A | HOH2404 |
| A | HOH2597 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM B 801 |
| Chain | Residue |
| B | HOH1313 |
| B | HOH1413 |
| B | HOH1566 |
| B | HOH1616 |
| B | HIS8 |
| B | VAL9 |
| B | CYS14 |
| B | CYS17 |
| B | HIS18 |
| B | LEU24 |
| B | SER73 |
| B | ALA74 |
| B | HIS75 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM B 802 |
| Chain | Residue |
| B | LEU4 |
| B | PHE7 |
| B | HIS8 |
| B | GLN12 |
| B | SER16 |
| B | GLN35 |
| B | CYS36 |
| B | CYS39 |
| B | HIS40 |
| B | HIS72 |
| B | TYR94 |
| B | HEM803 |
| B | HOH1835 |
| B | HOH1953 |
| B | HOH1958 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 803 |
| Chain | Residue |
| B | HIS40 |
| B | LEU43 |
| B | HIS52 |
| B | ALA57 |
| B | HIS58 |
| B | VAL66 |
| B | ALA67 |
| B | CYS68 |
| B | CYS71 |
| B | HIS72 |
| B | PHE90 |
| B | ASN91 |
| B | MET92 |
| B | HEM802 |
| B | HEM804 |
| B | HOH1240 |
| B | HOH1247 |
| B | HOH1890 |
| B | HOH2172 |
| site_id | BC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 804 |
| Chain | Residue |
| B | HIS54 |
| B | ASN56 |
| B | SER60 |
| B | HIS61 |
| B | PHE62 |
| B | CYS82 |
| B | SER84 |
| B | CYS85 |
| B | HIS86 |
| B | PHE88 |
| B | LEU167 |
| B | VAL374 |
| B | LYS431 |
| B | LYS434 |
| B | HEM803 |
| B | HOH1198 |
| B | HOH1199 |
| B | HOH1221 |
| B | HOH1253 |
| B | HOH1382 |
| B | HOH1605 |
| B | HOH1692 |
| B | HOH1829 |
| site_id | BC2 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FAD A 1805 |
| Chain | Residue |
| A | GLY133 |
| A | GLY135 |
| A | GLY136 |
| A | ALA137 |
| A | GLU156 |
| A | LYS157 |
| A | GLU158 |
| A | GLY162 |
| A | GLY163 |
| A | ASN164 |
| A | ALA165 |
| A | LEU167 |
| A | ALA168 |
| A | ALA169 |
| A | GLY170 |
| A | GLY171 |
| A | THR276 |
| A | ARG277 |
| A | GLY278 |
| A | ALA312 |
| A | THR313 |
| A | GLY314 |
| A | THR336 |
| A | GLN338 |
| A | ASP344 |
| A | MET375 |
| A | HIS504 |
| A | HIS505 |
| A | GLY533 |
| A | GLU534 |
| A | ARG544 |
| A | GLY547 |
| A | ASN548 |
| A | ALA549 |
| A | ILE550 |
| A | ILE553 |
| A | FUM1806 |
| A | HOH1819 |
| A | HOH1850 |
| A | HOH1853 |
| A | HOH1891 |
| site_id | BC3 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE FAD B 2805 |
| Chain | Residue |
| B | VAL132 |
| B | GLY133 |
| B | GLY135 |
| B | GLY136 |
| B | ALA137 |
| B | GLU156 |
| B | LYS157 |
| B | GLU158 |
| B | GLY162 |
| B | GLY163 |
| B | ASN164 |
| B | ALA165 |
| B | LEU167 |
| B | ALA168 |
| B | ALA169 |
| B | GLY170 |
| B | GLY171 |
| B | ARG277 |
| B | GLY278 |
| B | ALA312 |
| B | THR313 |
| B | GLY314 |
| B | THR336 |
| B | GLN338 |
| B | ASP344 |
| B | MET375 |
| B | HIS504 |
| B | HIS505 |
| B | GLY533 |
| B | GLU534 |
| B | ARG544 |
| B | GLY547 |
| B | ASN548 |
| B | ALA549 |
| B | ILE550 |
| B | ILE553 |
| B | HOH1008 |
| B | HOH1014 |
| B | HOH1037 |
| B | HOH1104 |
| B | HOH1144 |
| B | FUM2806 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FUM A 1806 |
| Chain | Residue |
| A | GLY170 |
| A | HIS365 |
| A | MET375 |
| A | THR377 |
| A | GLU378 |
| A | TYR402 |
| A | HIS504 |
| A | ARG544 |
| A | GLY546 |
| A | GLY547 |
| A | FAD1805 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FUM B 2806 |
| Chain | Residue |
| B | GLY170 |
| B | HIS365 |
| B | MET375 |
| B | THR377 |
| B | GLU378 |
| B | TYR402 |
| B | HIS504 |
| B | ARG544 |
| B | GLY546 |
| B | GLY547 |
| B | FAD2805 |
Functional Information from PROSITE/UniProt
| site_id | PS00028 |
| Number of Residues | 23 |
| Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cvs..ChgtLaevaettkHehynaH |
| Chain | Residue | Details |
| A | CYS36-HIS58 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10978153","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10978153","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E39","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"10978153","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E39","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10978153","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E39","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 46 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 48 |
| Details | Signal: {"evidences":[{"source":"PubMed","id":"1333793","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0C278","evidenceCode":"ECO:0000250"}]} |
