Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0005524 | molecular_function | ATP binding |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006457 | biological_process | protein folding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006457 | biological_process | protein folding |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| G | 0051082 | molecular_function | unfolded protein binding |
| G | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006457 | biological_process | protein folding |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0051082 | molecular_function | unfolded protein binding |
| H | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1527 |
| Chain | Residue |
| A | ASP95 |
| A | LYS165 |
| A | ADP1528 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 2527 |
| Chain | Residue |
| B | ASP95 |
| B | ADP2528 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 3527 |
| Chain | Residue |
| C | ASP95 |
| C | LYS165 |
| C | ADP3528 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 4527 |
| Chain | Residue |
| D | LYS165 |
| D | ADP4528 |
| D | ASP95 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 5527 |
| Chain | Residue |
| E | ASP95 |
| E | LYS165 |
| E | ADP5528 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG G 6527 |
| Chain | Residue |
| G | ASP95 |
| G | ADP7528 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG H 8527 |
| Chain | Residue |
| H | ASP95 |
| H | LYS165 |
| H | ADP8528 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP A 1528 |
| Chain | Residue |
| A | THR42 |
| A | GLY44 |
| A | PRO45 |
| A | ASN63 |
| A | ASP95 |
| A | GLY96 |
| A | THR97 |
| A | THR98 |
| A | THR99 |
| A | GLY164 |
| A | ALA410 |
| A | GLY411 |
| A | LEU451 |
| A | ILE479 |
| A | ASP480 |
| A | VAL481 |
| A | PHE482 |
| A | GLU496 |
| A | MG1527 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP B 2528 |
| Chain | Residue |
| B | THR42 |
| B | LEU43 |
| B | GLY44 |
| B | PRO45 |
| B | ASN63 |
| B | ASP95 |
| B | GLY96 |
| B | THR97 |
| B | THR98 |
| B | THR99 |
| B | GLY164 |
| B | ALA410 |
| B | GLY411 |
| B | LEU451 |
| B | ILE479 |
| B | ASP480 |
| B | VAL481 |
| B | ILE494 |
| B | GLU496 |
| B | MG2527 |
| site_id | BC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP C 3528 |
| Chain | Residue |
| C | THR42 |
| C | LEU43 |
| C | GLY44 |
| C | PRO45 |
| C | ASN63 |
| C | ASP95 |
| C | GLY96 |
| C | THR97 |
| C | THR98 |
| C | THR99 |
| C | GLY164 |
| C | ALA410 |
| C | GLY411 |
| C | LEU451 |
| C | ILE479 |
| C | ASP480 |
| C | VAL481 |
| C | PHE482 |
| C | GLU496 |
| C | LYS501 |
| C | MG3527 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP D 4528 |
| Chain | Residue |
| D | THR42 |
| D | GLY44 |
| D | PRO45 |
| D | ASN63 |
| D | ASP95 |
| D | GLY96 |
| D | THR97 |
| D | THR98 |
| D | THR99 |
| D | GLY164 |
| D | ALA410 |
| D | GLY411 |
| D | LEU451 |
| D | ILE479 |
| D | ASP480 |
| D | VAL481 |
| D | PHE482 |
| D | ILE494 |
| D | GLU496 |
| D | MG4527 |
| site_id | BC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP E 5528 |
| Chain | Residue |
| E | THR42 |
| E | LEU43 |
| E | GLY44 |
| E | PRO45 |
| E | ASN63 |
| E | ASP95 |
| E | GLY96 |
| E | THR97 |
| E | THR98 |
| E | THR99 |
| E | GLY164 |
| E | ALA410 |
| E | GLY411 |
| E | GLY412 |
| E | ILE447 |
| E | LEU451 |
| E | ILE479 |
| E | ASP480 |
| E | VAL481 |
| E | PHE482 |
| E | ILE494 |
| E | GLU496 |
| E | LYS501 |
| E | MG5527 |
| site_id | BC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP F 6528 |
| Chain | Residue |
| F | THR42 |
| F | LEU43 |
| F | GLY44 |
| F | PRO45 |
| F | ASN63 |
| F | ASP95 |
| F | GLY96 |
| F | THR97 |
| F | THR98 |
| F | THR99 |
| F | GLY164 |
| F | ALA410 |
| F | GLY411 |
| F | LEU451 |
| F | ILE479 |
| F | ASP480 |
| F | VAL481 |
| F | PHE482 |
| F | GLU496 |
| F | LYS501 |
| site_id | BC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP G 7528 |
| Chain | Residue |
| G | THR42 |
| G | LEU43 |
| G | GLY44 |
| G | PRO45 |
| G | ASN63 |
| G | ASP95 |
| G | GLY96 |
| G | THR97 |
| G | THR98 |
| G | THR99 |
| G | GLY164 |
| G | ALA410 |
| G | GLY411 |
| G | ILE447 |
| G | LEU451 |
| G | ILE479 |
| G | ASP480 |
| G | VAL481 |
| G | PHE482 |
| G | ILE494 |
| G | GLU496 |
| G | MG6527 |
| site_id | BC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP H 8528 |
| Chain | Residue |
| H | THR42 |
| H | LEU43 |
| H | GLY44 |
| H | PRO45 |
| H | ASN63 |
| H | ASP95 |
| H | GLY96 |
| H | THR97 |
| H | THR98 |
| H | THR99 |
| H | GLY164 |
| H | ALA410 |
| H | GLY411 |
| H | ILE447 |
| H | LEU451 |
| H | ILE479 |
| H | ASP480 |
| H | VAL481 |
| H | PHE482 |
| H | ILE494 |
| H | GLU496 |
| H | MG8527 |
Functional Information from PROSITE/UniProt
| site_id | PS00750 |
| Number of Residues | 13 |
| Details | TCP1_1 Chaperonins TCP-1 signature 1. RTtLGPkGmdKML |
| Chain | Residue | Details |
| A | ARG40-LEU52 | |
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QDkeAGDGT |
| Chain | Residue | Details |
| A | GLN89-THR97 | |
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 | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| E | THR98 | |
| E | THR97 | |
| E | ASP64 | |
| E | ASP393 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| F | THR98 | |
| F | THR97 | |
| F | ASP64 | |
| F | ASP393 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| G | THR98 | |
| G | THR97 | |
| G | ASP64 | |
| G | ASP393 | |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| H | THR98 | |
| H | THR97 | |
| H | ASP64 | |
| H | 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 |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| E | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| E | THR97 | electrostatic stabiliser, hydrogen bond donor |
| E | THR98 | electrostatic stabiliser, hydrogen bond donor |
| E | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| F | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| F | THR97 | electrostatic stabiliser, hydrogen bond donor |
| F | THR98 | electrostatic stabiliser, hydrogen bond donor |
| F | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| G | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| G | THR97 | electrostatic stabiliser, hydrogen bond donor |
| G | THR98 | electrostatic stabiliser, hydrogen bond donor |
| G | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 179 |
| Chain | Residue | Details |
| H | ASP64 | electrostatic stabiliser, hydrogen bond acceptor |
| H | THR97 | electrostatic stabiliser, hydrogen bond donor |
| H | THR98 | electrostatic stabiliser, hydrogen bond donor |
| H | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
