Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006457 | biological_process | protein folding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009408 | biological_process | response to heat |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| A | 0048039 | molecular_function | ubiquinone binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006457 | biological_process | protein folding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009408 | biological_process | response to heat |
| D | 0015035 | molecular_function | protein-disulfide reductase activity |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| D | 0048039 | molecular_function | ubiquinone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UQ8 A 201 |
| Chain | Residue |
| A | ALA29 |
| A | PRO143 |
| A | LEU38 |
| A | PRO40 |
| A | SER41 |
| A | CYS44 |
| A | GLU47 |
| A | ARG48 |
| A | HIS91 |
| A | MET142 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UQ8 D 201 |
| Chain | Residue |
| D | LEU38 |
| D | PRO40 |
| D | CYS44 |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| B | TYR217-HIS223 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 96 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 734 |
| Chain | Residue | Details |
| A | SER41 | electrofuge, electrophile, nucleofuge, nucleophile |
| A | CYS44 | electrofuge, electrophile, nucleofuge, nucleophile |
| A | ARG48 | electrostatic stabiliser |
| A | CYS104 | covalently attached, nucleofuge, nucleophile |
| A | CYS130 | electrofuge, electrophile, nucleophile |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 734 |
| Chain | Residue | Details |
| D | SER41 | electrofuge, electrophile, nucleofuge, nucleophile |
| D | CYS44 | electrofuge, electrophile, nucleofuge, nucleophile |
| D | ARG48 | electrostatic stabiliser |
| D | CYS104 | covalently attached, nucleofuge, nucleophile |
| D | CYS130 | electrofuge, electrophile, nucleophile |
