4XCI
Crystal structure of a hexadecameric TF55 complex from S. solfataricus, crystal form II
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006457 | biological_process | protein folding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0051082 | molecular_function | unfolded protein binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005832 | cellular_component | chaperonin-containing T-complex |
B | 0006457 | biological_process | protein folding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0051082 | molecular_function | unfolded protein binding |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PROSITE/UniProt
site_id | PS00750 |
Number of Residues | 13 |
Details | TCP1_1 Chaperonins TCP-1 signature 1. KStYGPrGmdKML |
Chain | Residue | Details |
B | LYS49-LEU61 | |
A | ARG36-LEU48 |
site_id | PS00995 |
Number of Residues | 9 |
Details | TCP1_3 Chaperonins TCP-1 signature 3. QDeeTADGT |
Chain | Residue | Details |
B | GLN98-THR106 | |
A | GLN85-THR93 |
site_id | PS00751 |
Number of Residues | 17 |
Details | TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATILdkMdLqHP |
Chain | Residue | Details |
B | ILE70-PRO86 | |
A | ILE57-PRO73 |