Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0016972 | molecular_function | thiol oxidase activity |
| A | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| A | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NEN A 501 |
| Chain | Residue |
| A | GLN205 |
| A | CYS208 |
| A | MET258 |
| A | ASN263 |
| A | TYR420 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FAD A 1 |
| Chain | Residue |
| A | THR189 |
| A | GLY190 |
| A | TYR191 |
| A | GLY192 |
| A | ALA196 |
| A | ILE199 |
| A | TRP200 |
| A | TYR204 |
| A | SER228 |
| A | HIS231 |
| A | ALA232 |
| A | ILE234 |
| A | ARG260 |
| A | ARG267 |
| A | MET347 |
| A | CYS355 |
| A | HOH10 |
| A | ASP108 |
| A | ARG187 |
| A | PHE188 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD A 432 |
| Chain | Residue |
| A | GLU241 |
| A | GLU408 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15163408","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"15163408","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15163408","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
