1Q6H
Crystal structure of a truncated form of FkpA from Escherichia coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
A | 0006457 | biological_process | protein folding |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042026 | biological_process | protein refolding |
A | 0042597 | cellular_component | periplasmic space |
A | 0044183 | molecular_function | protein folding chaperone |
B | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
B | 0006457 | biological_process | protein folding |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042026 | biological_process | protein refolding |
B | 0042597 | cellular_component | periplasmic space |
B | 0044183 | molecular_function | protein folding chaperone |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1d6o |
Chain | Residue | Details |
A | TYR200 | |
A | ILE174 | |
A | ASP157 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1d6o |
Chain | Residue | Details |
B | TYR200 | |
B | ILE174 | |
B | ASP157 |