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 | 0016853 | molecular_function | isomerase activity |
| 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 | 0006457 | biological_process | protein folding |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue ADP B 600 |
| Chain | Residue |
| B | THR51 |
| B | GLY420 |
| B | GLY421 |
| B | LEU489 |
| B | VAL504 |
| B | GLU506 |
| B | LYS511 |
| B | TYR52 |
| B | GLY53 |
| B | PRO54 |
| B | ASP104 |
| B | LYS107 |
| B | THR169 |
| B | SER170 |
| B | GLY419 |
Functional Information from PROSITE/UniProt
| site_id | PS00750 |
| Number of Residues | 13 |
| Details | TCP1_1 Chaperonins TCP-1 signature 1. RSsLGPkGldKML |
| Chain | Residue | Details |
| A | ARG36-LEU48 | |
| B | LYS49-LEU61 | |
| site_id | PS00751 |
| Number of Residues | 17 |
| Details | TCP1_2 Chaperonins TCP-1 signature 2. ITNDGATIVkdMeIqHP |
| Chain | Residue | Details |
| A | ILE57-PRO73 | |
| B | ILE70-PRO86 | |
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QDaeVGDGT |
| Chain | Residue | Details |
| A | GLN85-THR93 | |
| B | GLN98-THR106 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4XCD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6XHI","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6XHJ","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33682792","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6XHJ","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26853941","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4XCD","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4XCD","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33682792","evidenceCode":"ECO:0000269"}]} |
