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 | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | LYS277 | |
A | LYS321 | |
B | LYS277 | |
B | LYS321 | |
C | LYS277 | |
C | LYS321 |