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 | 0016853 | molecular_function | isomerase activity |
| 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 | 0016853 | molecular_function | isomerase activity |
| 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 |
