6KS6
TRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| a | 0005515 | molecular_function | protein binding |
| a | 0005524 | molecular_function | ATP binding |
| a | 0005737 | cellular_component | cytoplasm |
| a | 0005832 | cellular_component | chaperonin-containing T-complex |
| a | 0005886 | cellular_component | plasma membrane |
| a | 0006457 | biological_process | protein folding |
| a | 0016887 | molecular_function | ATP hydrolysis activity |
| a | 0051082 | molecular_function | unfolded protein binding |
| a | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| a | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005832 | cellular_component | chaperonin-containing T-complex |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| b | 0005515 | molecular_function | protein binding |
| b | 0005524 | molecular_function | ATP binding |
| b | 0005737 | cellular_component | cytoplasm |
| b | 0005829 | cellular_component | cytosol |
| b | 0005832 | cellular_component | chaperonin-containing T-complex |
| b | 0006457 | biological_process | protein folding |
| b | 0016887 | molecular_function | ATP hydrolysis activity |
| b | 0051082 | molecular_function | unfolded protein binding |
| b | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| b | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005832 | cellular_component | chaperonin-containing T-complex |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| d | 0005524 | molecular_function | ATP binding |
| d | 0005737 | cellular_component | cytoplasm |
| d | 0005832 | cellular_component | chaperonin-containing T-complex |
| d | 0006457 | biological_process | protein folding |
| d | 0016887 | molecular_function | ATP hydrolysis activity |
| d | 0051082 | molecular_function | unfolded protein binding |
| d | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| d | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005832 | cellular_component | chaperonin-containing T-complex |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| e | 0005524 | molecular_function | ATP binding |
| e | 0005737 | cellular_component | cytoplasm |
| e | 0005832 | cellular_component | chaperonin-containing T-complex |
| e | 0006457 | biological_process | protein folding |
| e | 0016887 | molecular_function | ATP hydrolysis activity |
| e | 0051082 | molecular_function | unfolded protein binding |
| e | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| e | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005832 | cellular_component | chaperonin-containing T-complex |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| E | 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 |
| 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 | 0005737 | cellular_component | cytoplasm |
| h | 0005832 | cellular_component | chaperonin-containing T-complex |
| h | 0006457 | biological_process | protein folding |
| h | 0016887 | molecular_function | ATP hydrolysis activity |
| h | 0051082 | molecular_function | unfolded protein binding |
| h | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| h | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005832 | cellular_component | chaperonin-containing T-complex |
| H | 0006457 | biological_process | protein folding |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0051082 | molecular_function | unfolded protein binding |
| H | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| H | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| q | 0005524 | molecular_function | ATP binding |
| q | 0005737 | cellular_component | cytoplasm |
| q | 0005832 | cellular_component | chaperonin-containing T-complex |
| q | 0006457 | biological_process | protein folding |
| q | 0016887 | molecular_function | ATP hydrolysis activity |
| q | 0051082 | molecular_function | unfolded protein binding |
| q | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| q | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| Q | 0005524 | molecular_function | ATP binding |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0005832 | cellular_component | chaperonin-containing T-complex |
| Q | 0006457 | biological_process | protein folding |
| Q | 0016887 | molecular_function | ATP hydrolysis activity |
| Q | 0051082 | molecular_function | unfolded protein binding |
| Q | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| Q | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| z | 0005524 | molecular_function | ATP binding |
| z | 0005737 | cellular_component | cytoplasm |
| z | 0005832 | cellular_component | chaperonin-containing T-complex |
| z | 0006457 | biological_process | protein folding |
| z | 0016887 | molecular_function | ATP hydrolysis activity |
| z | 0051082 | molecular_function | unfolded protein binding |
| z | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| z | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| Z | 0005524 | molecular_function | ATP binding |
| Z | 0005737 | cellular_component | cytoplasm |
| Z | 0005832 | cellular_component | chaperonin-containing T-complex |
| Z | 0006457 | biological_process | protein folding |
| Z | 0016887 | molecular_function | ATP hydrolysis activity |
| Z | 0051082 | molecular_function | unfolded protein binding |
| Z | 0051086 | biological_process | chaperone mediated protein folding independent of cofactor |
| Z | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ADP a 601 |
| Chain | Residue |
| a | PRO46 |
| a | LEU502 |
| a | VAL517 |
| a | MG602 |
| a | AF3603 |
| a | ASP96 |
| a | GLY97 |
| a | THR99 |
| a | THR162 |
| a | SER165 |
| a | SER166 |
| a | GLY421 |
| a | GLY422 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG a 602 |
| Chain | Residue |
| a | ASP96 |
| a | ADP601 |
| a | AF3603 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 a 603 |
| Chain | Residue |
| a | ASP65 |
| a | ASP96 |
| a | THR98 |
| a | THR99 |
| a | LYS167 |
| a | ASP404 |
| a | ADP601 |
| a | MG602 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue ADP A 601 |
| Chain | Residue |
| A | LEU44 |
| A | PRO46 |
| A | GLY97 |
| A | THR98 |
| A | THR99 |
| A | SER100 |
| A | THR162 |
| A | SER165 |
| A | SER166 |
| A | GLY421 |
| A | GLY422 |
| A | VAL517 |
| A | GLU519 |
| A | MG602 |
| A | AF3603 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 602 |
| Chain | Residue |
| A | ASP96 |
| A | LYS167 |
| A | ADP601 |
| A | AF3603 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 A 603 |
| Chain | Residue |
| A | ASP65 |
| A | GLY66 |
| A | THR98 |
| A | THR99 |
| A | LYS167 |
| A | ASP404 |
| A | ADP601 |
| A | MG602 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue ADP b 601 |
| Chain | Residue |
| b | LEU37 |
| b | ASP90 |
| b | GLY91 |
| b | THR93 |
| b | SER94 |
| b | THR159 |
| b | SER162 |
| b | SER163 |
| b | GLY404 |
| b | GLY405 |
| b | GLU408 |
| b | LEU444 |
| b | ILE487 |
| b | GLU489 |
| b | MG602 |
| b | AF3603 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue MG b 602 |
| Chain | Residue |
| b | ASP90 |
| b | ADP601 |
| b | AF3603 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue AF3 b 603 |
| Chain | Residue |
| b | ASN58 |
| b | ASP59 |
| b | ASP90 |
| b | GLY91 |
| b | THR92 |
| b | THR93 |
| b | LYS164 |
| b | ASP386 |
| b | ADP601 |
| b | MG602 |
| site_id | AD1 |
| Number of Residues | 18 |
| Details | binding site for residue ADP B 601 |
| Chain | Residue |
| B | THR36 |
| B | LEU37 |
| B | GLY38 |
| B | PRO39 |
| B | ASP90 |
| B | GLY91 |
| B | THR92 |
| B | THR93 |
| B | SER94 |
| B | SER162 |
| B | SER163 |
| B | GLY404 |
| B | LEU444 |
| B | LEU472 |
| B | ILE487 |
| B | GLU489 |
| B | MG602 |
| B | AF3603 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 602 |
| Chain | Residue |
| B | SER163 |
| B | ADP601 |
| B | AF3603 |
| B | ASP90 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 B 603 |
| Chain | Residue |
| B | ASP59 |
| B | ASP90 |
| B | THR92 |
| B | THR93 |
| B | LYS164 |
| B | ASP386 |
| B | ADP601 |
| B | MG602 |
| site_id | AD4 |
| Number of Residues | 19 |
| Details | binding site for residue ADP d 601 |
| Chain | Residue |
| d | LEU39 |
| d | GLY40 |
| d | PRO41 |
| d | ASP91 |
| d | GLY92 |
| d | THR93 |
| d | THR94 |
| d | SER95 |
| d | THR156 |
| d | SER157 |
| d | SER159 |
| d | GLY413 |
| d | GLY414 |
| d | ILE482 |
| d | VAL484 |
| d | ILE497 |
| d | GLN499 |
| d | MG602 |
| d | AF3603 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue MG d 602 |
| Chain | Residue |
| d | ASP91 |
| d | SER157 |
| d | ADP601 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue AF3 d 603 |
| Chain | Residue |
| d | ASP60 |
| d | THR93 |
| d | THR94 |
| d | LYS161 |
| d | ASP396 |
| d | ADP601 |
| site_id | AD7 |
| Number of Residues | 18 |
| Details | binding site for residue ADP D 601 |
| Chain | Residue |
| D | LEU39 |
| D | GLY40 |
| D | PRO41 |
| D | ASP91 |
| D | GLY92 |
| D | THR93 |
| D | THR94 |
| D | THR156 |
| D | SER159 |
| D | SER160 |
| D | LYS161 |
| D | GLY414 |
| D | LEU454 |
| D | ILE482 |
| D | VAL484 |
| D | ILE497 |
| D | MG602 |
| D | AF3603 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue MG D 602 |
| Chain | Residue |
| D | ASP91 |
| D | SER157 |
| D | ADP601 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 D 603 |
| Chain | Residue |
| D | ASN59 |
| D | ASP60 |
| D | GLY61 |
| D | THR93 |
| D | THR94 |
| D | LYS161 |
| D | ASP396 |
| D | ADP601 |
| site_id | AE1 |
| Number of Residues | 17 |
| Details | binding site for residue ADP e 601 |
| Chain | Residue |
| e | LEU65 |
| e | GLY66 |
| e | PRO67 |
| e | ASP117 |
| e | GLY118 |
| e | THR119 |
| e | THR120 |
| e | THR186 |
| e | SER187 |
| e | SER190 |
| e | GLY442 |
| e | GLY443 |
| e | VAL527 |
| e | ASP529 |
| e | LYS534 |
| e | MG602 |
| e | AF3603 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue MG e 602 |
| Chain | Residue |
| e | ASP117 |
| e | ADP601 |
| e | AF3603 |
| site_id | AE3 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 e 603 |
| Chain | Residue |
| e | ASP86 |
| e | ASP117 |
| e | THR119 |
| e | THR120 |
| e | LYS191 |
| e | ASP425 |
| e | ADP601 |
| e | MG602 |
| site_id | AE4 |
| Number of Residues | 15 |
| Details | binding site for residue ADP E 601 |
| Chain | Residue |
| E | GLY66 |
| E | ASP117 |
| E | GLY118 |
| E | THR119 |
| E | THR120 |
| E | GLY189 |
| E | SER190 |
| E | GLY442 |
| E | GLY443 |
| E | LEU515 |
| E | VAL527 |
| E | ASP529 |
| E | LYS534 |
| E | MG602 |
| E | AF3603 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue MG E 602 |
| Chain | Residue |
| E | ASP117 |
| E | ADP601 |
| E | AF3603 |
| site_id | AE6 |
| Number of Residues | 7 |
| Details | binding site for residue AF3 E 603 |
| Chain | Residue |
| E | ASP86 |
| E | THR119 |
| E | THR120 |
| E | LYS191 |
| E | ASP425 |
| E | ADP601 |
| E | MG602 |
| site_id | AE7 |
| Number of Residues | 15 |
| Details | binding site for residue ADP g 601 |
| Chain | Residue |
| g | LEU39 |
| g | PRO41 |
| g | GLY92 |
| g | THR93 |
| g | THR94 |
| g | THR95 |
| g | SER158 |
| g | THR161 |
| g | GLY476 |
| g | ILE544 |
| g | GLY546 |
| g | ILE559 |
| g | GLU561 |
| g | MG602 |
| g | AF3603 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue MG g 602 |
| Chain | Residue |
| g | ASP91 |
| g | ADP601 |
| g | AF3603 |
| site_id | AE9 |
| Number of Residues | 9 |
| Details | binding site for residue AF3 g 603 |
| Chain | Residue |
| g | ASP60 |
| g | GLY61 |
| g | GLY90 |
| g | THR93 |
| g | THR94 |
| g | LYS162 |
| g | ADP601 |
| g | MG602 |
| g | HOH701 |
| site_id | AF1 |
| Number of Residues | 20 |
| Details | binding site for residue ADP G 601 |
| Chain | Residue |
| G | LEU39 |
| G | PRO41 |
| G | ASP91 |
| G | GLY92 |
| G | THR93 |
| G | THR94 |
| G | THR95 |
| G | SER158 |
| G | THR161 |
| G | GLY475 |
| G | GLY476 |
| G | GLY477 |
| G | LEU516 |
| G | ILE544 |
| G | GLY546 |
| G | TYR557 |
| G | GLU561 |
| G | LYS566 |
| G | MG602 |
| G | AF3603 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue MG G 602 |
| Chain | Residue |
| G | ASP91 |
| G | SER158 |
| G | ADP601 |
| G | AF3603 |
| site_id | AF3 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 G 603 |
| Chain | Residue |
| G | ASP60 |
| G | ASP91 |
| G | THR93 |
| G | THR94 |
| G | LYS162 |
| G | ASP458 |
| G | ADP601 |
| G | MG602 |
| site_id | AF4 |
| Number of Residues | 11 |
| Details | binding site for residue ADP h 601 |
| Chain | Residue |
| h | LEU44 |
| h | GLY45 |
| h | PRO46 |
| h | ASP96 |
| h | GLY97 |
| h | SER167 |
| h | SER168 |
| h | GLY413 |
| h | GLU498 |
| h | MG602 |
| h | AF3603 |
| site_id | AF5 |
| Number of Residues | 3 |
| Details | binding site for residue MG h 602 |
| Chain | Residue |
| h | ASP96 |
| h | ADP601 |
| h | AF3603 |
| site_id | AF6 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 h 603 |
| Chain | Residue |
| h | ASP65 |
| h | GLY95 |
| h | THR98 |
| h | THR99 |
| h | LYS169 |
| h | ASP395 |
| h | ADP601 |
| h | MG602 |
| site_id | AF7 |
| Number of Residues | 16 |
| Details | binding site for residue ADP H 601 |
| Chain | Residue |
| H | LEU44 |
| H | ASP96 |
| H | GLY97 |
| H | THR98 |
| H | THR99 |
| H | SER100 |
| H | SER167 |
| H | SER168 |
| H | GLY412 |
| H | GLY413 |
| H | LEU453 |
| H | PHE483 |
| H | GLU498 |
| H | LYS503 |
| H | MG602 |
| H | AF3603 |
| site_id | AF8 |
| Number of Residues | 3 |
| Details | binding site for residue MG H 602 |
| Chain | Residue |
| H | ASP96 |
| H | ADP601 |
| H | AF3603 |
| site_id | AF9 |
| Number of Residues | 7 |
| Details | binding site for residue AF3 H 603 |
| Chain | Residue |
| H | ASP65 |
| H | GLY95 |
| H | THR98 |
| H | THR99 |
| H | ASP395 |
| H | ADP601 |
| H | MG602 |
| site_id | AG1 |
| Number of Residues | 13 |
| Details | binding site for residue ADP q 601 |
| Chain | Residue |
| q | MET46 |
| q | PRO48 |
| q | ASP98 |
| q | GLY99 |
| q | SER168 |
| q | SER169 |
| q | TYR172 |
| q | GLY422 |
| q | ALA423 |
| q | LEU463 |
| q | ILE517 |
| q | ASP519 |
| q | MG602 |
| site_id | AG2 |
| Number of Residues | 5 |
| Details | binding site for residue MG q 602 |
| Chain | Residue |
| q | ASP98 |
| q | VAL166 |
| q | SER169 |
| q | LYS170 |
| q | ADP601 |
| site_id | AG3 |
| Number of Residues | 4 |
| Details | binding site for residue MG Q 601 |
| Chain | Residue |
| Q | ASP98 |
| Q | VAL166 |
| Q | SER169 |
| Q | ADP602 |
| site_id | AG4 |
| Number of Residues | 15 |
| Details | binding site for residue ADP Q 602 |
| Chain | Residue |
| Q | MET46 |
| Q | PRO48 |
| Q | ASP98 |
| Q | GLY99 |
| Q | THR100 |
| Q | ASN101 |
| Q | SER168 |
| Q | SER169 |
| Q | LYS170 |
| Q | GLY422 |
| Q | ALA423 |
| Q | VAL499 |
| Q | ILE517 |
| Q | ASP519 |
| Q | MG601 |
| site_id | AG5 |
| Number of Residues | 17 |
| Details | binding site for residue ADP z 601 |
| Chain | Residue |
| z | LEU37 |
| z | PRO39 |
| z | ASP89 |
| z | GLY90 |
| z | THR91 |
| z | THR92 |
| z | THR93 |
| z | THR160 |
| z | GLY414 |
| z | ALA415 |
| z | GLY416 |
| z | LEU458 |
| z | VAL491 |
| z | ILE506 |
| z | ASP508 |
| z | MG602 |
| z | AF3603 |
| site_id | AG6 |
| Number of Residues | 3 |
| Details | binding site for residue MG z 602 |
| Chain | Residue |
| z | ASP89 |
| z | ADP601 |
| z | AF3603 |
| site_id | AG7 |
| Number of Residues | 9 |
| Details | binding site for residue AF3 z 603 |
| Chain | Residue |
| z | ASP58 |
| z | ASP89 |
| z | THR91 |
| z | THR92 |
| z | LYS161 |
| z | ASP397 |
| z | ADP601 |
| z | MG602 |
| z | HOH701 |
| site_id | AG8 |
| Number of Residues | 14 |
| Details | binding site for residue ADP Z 601 |
| Chain | Residue |
| Z | LEU37 |
| Z | PRO39 |
| Z | ASP89 |
| Z | GLY90 |
| Z | THR92 |
| Z | THR93 |
| Z | THR160 |
| Z | GLY414 |
| Z | ALA415 |
| Z | GLY416 |
| Z | VAL491 |
| Z | ILE506 |
| Z | MG602 |
| Z | AF3603 |
| site_id | AG9 |
| Number of Residues | 3 |
| Details | binding site for residue MG Z 602 |
| Chain | Residue |
| Z | ASP89 |
| Z | ADP601 |
| Z | AF3603 |
| site_id | AH1 |
| Number of Residues | 8 |
| Details | binding site for residue AF3 Z 603 |
| Chain | Residue |
| Z | ASP58 |
| Z | THR91 |
| Z | THR92 |
| Z | LYS161 |
| Z | ASP397 |
| Z | ADP601 |
| Z | MG602 |
| Z | HOH701 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 34 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTIlAgelmkeakpfleegisshLIMK |
| Chain | Residue | Details |
| h | VAL94-LYS127 |
| site_id | PS00750 |
| Number of Residues | 13 |
| Details | TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkAmlKML |
| Chain | Residue | Details |
| g | ARG36-LEU48 | |
| b | LYS34-LEU46 | |
| q | LEU43-ILE55 | |
| d | ARG36-ILE48 | |
| z | GLU34-LEU46 | |
| a | LYS41-LEU53 | |
| e | LYS62-LEU74 |
| site_id | PS00751 |
| Number of Residues | 17 |
| Details | TCP1_2 Chaperonins TCP-1 signature 2. LTNDGHAILreIdVaHP |
| Chain | Residue | Details |
| g | LEU57-PRO73 | |
| b | VAL56-PRO72 | |
| q | ILE64-PRO80 | |
| h | ILE62-PRO78 | |
| d | ILE57-PRO73 | |
| z | LEU55-PRO71 | |
| a | VAL62-PRO78 |
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT |
| Chain | Residue | Details |
| g | GLN85-THR93 | |
| b | GLN84-THR92 | |
| q | GLN92-THR100 | |
| h | GLN90-THR98 | |
| d | GLN85-THR93 | |
| z | GLN83-THR91 | |
| a | GLN90-THR98 | |
| e | GLN111-THR119 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| z | SER2 | |
| Z | SER2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| z | SER249 | |
| Z | SER249 | |
| Q | LYS15 |
