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 |
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 | HOH1819 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM A 801 |
| Chain | Residue |
| A | CYS17 |
| A | HIS18 |
| A | LEU24 |
| A | SER73 |
| A | ALA74 |
| A | HIS75 |
| A | HOH1924 |
| A | HOH2018 |
| A | HOH2100 |
| A | HOH2417 |
| A | HIS8 |
| A | VAL9 |
| A | CYS14 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 802 |
| Chain | Residue |
| A | LEU4 |
| A | PHE7 |
| A | HIS8 |
| A | GLN12 |
| A | SER16 |
| A | GLN35 |
| A | CYS36 |
| A | CYS39 |
| A | HIS40 |
| A | HIS72 |
| A | TYR94 |
| A | HEM803 |
| A | HOH2165 |
| A | HOH2568 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 803 |
| Chain | Residue |
| A | HIS40 |
| A | LEU43 |
| A | VAL46 |
| 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 | HOH1885 |
| A | HOH1942 |
| A | HOH2192 |
| A | HOH2195 |
| A | HOH2222 |
| A | HOH2397 |
| site_id | AC5 |
| 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 | GLN338 |
| A | VAL374 |
| A | LYS431 |
| A | LYS434 |
| A | TYR435 |
| A | HEM803 |
| A | HOH1826 |
| A | HOH1870 |
| A | HOH1932 |
| A | HOH1944 |
| A | HOH2029 |
| A | HOH2116 |
| A | HOH2398 |
| site_id | AC6 |
| Number of Residues | 44 |
| Details | BINDING SITE FOR RESIDUE FAD A 1805 |
| Chain | Residue |
| A | GLY278 |
| A | ALA312 |
| A | THR313 |
| A | GLY314 |
| A | THR336 |
| A | ASN337 |
| 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 | HOH1813 |
| A | HOH1835 |
| A | HOH1842 |
| A | HOH1845 |
| A | HOH1852 |
| A | VAL132 |
| 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 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FUM A 1806 |
| Chain | Residue |
| A | GLY170 |
| A | MET236 |
| A | HIS365 |
| A | THR377 |
| A | GLU378 |
| A | ARG402 |
| A | HIS504 |
| A | ARG544 |
| A | GLY546 |
| A | GLY547 |
| A | FAD1805 |
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 | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10978153","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| 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 | 7 |
| 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 | 8 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 17 |
| 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 | 8 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 23 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P83223","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Signal: {"evidences":[{"source":"PubMed","id":"1333793","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0C278","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d4c |
| Chain | Residue | Details |
| A | HIS504 | |
| A | ARG544 | |
| A | HIS365 | |
| A | ARG402 | |
