Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | HIS120 |
| A | HIS125 |
| A | HIS157 |
| A | HIS161 |
| A | HIS301 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | HOH501 |
| A | HIS160 |
| A | HIS269 |
| A | HIS298 |
| A | HIS302 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | binding site for residue ST9 A 403 |
| Chain | Residue |
| A | VAL72 |
| A | ASN75 |
| A | ALA112 |
| A | ILE115 |
| A | THR116 |
| A | HIS120 |
| A | PHE146 |
| A | GLN147 |
| A | ASN148 |
| A | TRP153 |
| A | ARG155 |
| A | ASP156 |
| A | HIS157 |
| A | HIS171 |
| A | TRP184 |
| A | LEU185 |
| A | VAL187 |
| A | ARG188 |
| A | LYS189 |
| A | VAL193 |
| A | LYS194 |
| A | GLY197 |
| A | ARG215 |
| A | TYR254 |
| A | THR261 |
| A | TRP262 |
| A | VAL264 |
| A | ASN265 |
| A | ALA292 |
| A | VAL293 |
| A | GLU295 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue LMT A 404 |
| Chain | Residue |
| A | ALA60 |
| A | ASP61 |
| A | ALA62 |
| A | HIS167 |
| A | HIS190 |
| A | GLU195 |
| A | LYS196 |
Functional Information from PROSITE/UniProt
| site_id | PS00476 |
| Number of Residues | 15 |
| Details | FATTY_ACID_DESATUR_1 Fatty acid desaturases family 1 signature. GEgFHNYHHsFPyDY |
| Chain | Residue | Details |
| A | GLY294-TYR308 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"26098317","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"26098317","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 98 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26098317","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Motif: {"description":"Histidine box-1","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Histidine box-2","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Histidine box-3","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26098317","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26098317","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |