2HI7
Crystal structure of DsbA-DsbB-ubiquinone complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003756 | molecular_function | protein disulfide isomerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0071236 | biological_process | cellular response to antibiotic |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006457 | biological_process | protein folding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009408 | biological_process | response to heat |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| B | 0048039 | molecular_function | ubiquinone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 190 |
| Chain | Residue |
| A | GLU38 |
| A | GLU38 |
| A | HIS41 |
| A | HIS41 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UQ1 B 501 |
| Chain | Residue |
| B | GLU47 |
| B | ARG48 |
| B | HIS91 |
| B | MET142 |
| B | LEU146 |
| B | ALA29 |
| B | LYS39 |
| B | CYS41 |
| B | LEU43 |
| B | CYS44 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 130 |
| Details | Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 17 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 17110337 |
| Chain | Residue | Details |
| B | CYS44 | |
| B | ARG48 | |
| B | CYS104 | |
| B | CYS41 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 734 |
| Chain | Residue | Details |
| B | CYS41 | electrofuge, electrophile, nucleofuge, nucleophile |
| B | CYS44 | electrofuge, electrophile, nucleofuge, nucleophile |
| B | ARG48 | electrostatic stabiliser |
| B | CYS104 | covalently attached, nucleofuge, nucleophile |
