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 | 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 |
A | 0061077 | biological_process | chaperone-mediated protein folding |
B | 0003756 | molecular_function | protein disulfide isomerase activity |
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 |
B | 0061077 | biological_process | chaperone-mediated protein folding |
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 |
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 |