1Q2V
Crystal structure of the chaperonin from Thermococcus strain KS-1 (nucleotide-free form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide 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 | 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 | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006457 | biological_process | protein folding |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1527 |
| Chain | Residue |
| A | LEU43 |
| A | GLY96 |
| A | THR97 |
| A | THR98 |
| A | THR99 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2527 |
| Chain | Residue |
| B | THR99 |
| B | LEU43 |
| B | GLY96 |
| B | THR97 |
| B | THR98 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3527 |
| Chain | Residue |
| C | LEU43 |
| C | GLY96 |
| C | THR97 |
| C | THR98 |
| C | THR99 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 4527 |
| Chain | Residue |
| D | LEU43 |
| D | GLY96 |
| D | THR97 |
| D | THR98 |
| D | THR99 |
| D | HOH4561 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"14729342","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14729342","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q3S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14729342","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q3Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q3S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1Q3S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| A | THR98 | |
| A | THR97 | |
| A | ASP64 | |
| A | ASP393 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| B | THR98 | |
| B | THR97 | |
| B | ASP64 | |
| B | ASP393 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| C | THR98 | |
| C | THR97 | |
| C | ASP64 | |
| C | ASP393 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| D | THR98 | |
| D | THR97 | |
| D | ASP64 | |
| D | ASP393 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| A | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| A | THR97 | electrostatic stabiliser, hydrogen bond donor |
| A | THR98 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| B | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| B | THR97 | electrostatic stabiliser, hydrogen bond donor |
| B | THR98 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| C | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| C | THR97 | electrostatic stabiliser, hydrogen bond donor |
| C | THR98 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| D | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| D | THR97 | electrostatic stabiliser, hydrogen bond donor |
| D | THR98 | electrostatic stabiliser, hydrogen bond donor |
| D | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
