5OWI
The dynamic dimer structure of the chaperone Trigger Factor (conformer 1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006457 | biological_process | protein folding |
| A | 0009408 | biological_process | response to heat |
| A | 0015031 | biological_process | protein transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043022 | molecular_function | ribosome binding |
| A | 0043335 | biological_process | protein unfolding |
| A | 0044183 | molecular_function | protein folding chaperone |
| A | 0051083 | biological_process | 'de novo' cotranslational protein folding |
| A | 0051301 | biological_process | cell division |
| A | 1990169 | biological_process | stress response to copper ion |
| B | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006457 | biological_process | protein folding |
| B | 0009408 | biological_process | response to heat |
| B | 0015031 | biological_process | protein transport |
| B | 0016020 | cellular_component | membrane |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043022 | molecular_function | ribosome binding |
| B | 0043335 | biological_process | protein unfolding |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0051083 | biological_process | 'de novo' cotranslational protein folding |
| B | 0051301 | biological_process | cell division |
| B | 1990169 | biological_process | stress response to copper ion |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 170 |
| Details | Domain: {"description":"PPIase FKBP-type"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 222 |
| Details | Region: {"description":"Ribosome-binding","evidences":[{"source":"PubMed","id":"14726952","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 206 |
| Details | Region: {"description":"Dispensable for chaperone activity, although its removal significantly decreases antiaggregation activity","evidences":[{"source":"PubMed","id":"14726952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24812405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"ADP-ribosylarginine","evidences":[{"source":"PubMed","id":"16112649","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
