3VZ8
Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0042026 | biological_process | protein refolding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005524 | molecular_function | ATP binding |
| B | 0042026 | biological_process | protein refolding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0005524 | molecular_function | ATP binding |
| C | 0042026 | biological_process | protein refolding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






