1EEJ
CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003756 | molecular_function | protein disulfide isomerase activity |
| A | 0006457 | biological_process | protein folding |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046688 | biological_process | response to copper ion |
| B | 0003756 | molecular_function | protein disulfide isomerase activity |
| B | 0006457 | biological_process | protein folding |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046688 | biological_process | response to copper ion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 1001 |
| Chain | Residue |
| B | SER17 |
| B | LYS82 |
| B | PRO84 |
| B | GLN85 |
| B | GLU86 |
| B | ASP166 |
| B | ASP169 |
| B | HOH1111 |
Functional Information from PROSITE/UniProt
| site_id | PS00194 |
| Number of Residues | 19 |
| Details | THIOREDOXIN_1 Thioredoxin family active site. ITvFTdiTCGYCHkLheqM |
| Chain | Residue | Details |
| A | ILE90-MET108 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 390 |
| Details | Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 10700276 |
| Chain | Residue | Details |
| A | CYS98 | |
| A | TYR100 | |
| A | CYS101 | |
| A | ARG125 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 10700276 |
| Chain | Residue | Details |
| B | CYS98 | |
| B | TYR100 | |
| B | CYS101 | |
| B | ARG125 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 512 |
| Chain | Residue | Details |
| A | ASP95 | increase nucleophilicity, proton acceptor, proton donor |
| A | CYS98 | electrofuge, electrophile, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | CYS101 | nucleophile, proton donor |
| A | ARG125 | increase nucleophilicity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 512 |
| Chain | Residue | Details |
| B | ASP95 | increase nucleophilicity, proton acceptor, proton donor |
| B | CYS98 | electrofuge, electrophile, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | CYS101 | nucleophile, proton donor |
| B | ARG125 | increase nucleophilicity |
