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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 997 |
Chain | Residue |
B | ASP93 |
B | ADP998 |
B | AF3999 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 897 |
Chain | Residue |
A | ASP94 |
A | ADP898 |
A | AF3899 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ADP B 998 |
Chain | Residue |
B | SER40 |
B | LEU41 |
B | GLY42 |
B | PRO43 |
B | ASP93 |
B | GLY94 |
B | THR96 |
B | THR97 |
B | THR158 |
B | SER162 |
B | GLY408 |
B | GLY409 |
B | LEU449 |
B | ILE477 |
B | PHE480 |
B | MET487 |
B | VAL492 |
B | GLU494 |
B | MG997 |
B | AF3999 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AF3 B 999 |
Chain | Residue |
B | ASN61 |
B | GLY63 |
B | ASP93 |
B | THR95 |
B | THR96 |
B | LYS163 |
B | ASP391 |
B | HOH951 |
B | MG997 |
B | ADP998 |
site_id | AC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP A 898 |
Chain | Residue |
A | THR41 |
A | LEU42 |
A | GLY43 |
A | PRO44 |
A | ASP94 |
A | GLY95 |
A | THR96 |
A | THR97 |
A | THR98 |
A | THR157 |
A | SER160 |
A | GLY407 |
A | GLY408 |
A | LEU448 |
A | LEU478 |
A | VAL491 |
A | ASP493 |
A | MG897 |
A | AF3899 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AF3 A 899 |
Chain | Residue |
A | ASN62 |
A | ASP63 |
A | GLY64 |
A | ASP94 |
A | THR96 |
A | THR97 |
A | ASP390 |
A | MG897 |
A | ADP898 |
A | HOH950 |
site_id | ASB |
Number of Residues | 11 |
Details | RESIDUE NUMBERING ACCORDING TO ALPHA-TYPE SUBUNIT. |
Chain | Residue |
B | GLY42 |
B | PRO43 |
B | ARG44 |
B | GLY63 |
B | GLY94 |
B | THR96 |
B | THR97 |
B | ALA98 |
B | GLN157 |
B | THR390 |
B | ILE493 |
site_id | ASE |
Number of Residues | 11 |
Details | RESIDUE NUMBERING ACCORDING TO ALPHA-TYPE SUBUNIT. |
Chain | Residue |
A | LEU42 |
A | ASP390 |
A | ASP493 |
A | GLY43 |
A | PRO44 |
A | ASP63 |
A | ASP94 |
A | THR96 |
A | THR97 |
A | THR98 |
A | THR157 |
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 | ARG39-LEU51 | |
B | ARG38-LEU50 | |
site_id | PS00751 |
Number of Residues | 17 |
Details | TCP1_2 Chaperonins TCP-1 signature 2. ISNDGATILkeMdVeHP |
Chain | Residue | Details |
A | ILE60-PRO76 | |
B | ILE59-PRO75 | |
site_id | PS00995 |
Number of Residues | 9 |
Details | TCP1_3 Chaperonins TCP-1 signature 3. QDtaVGDGT |
Chain | Residue | Details |
A | GLN88-THR96 | |
B | GLN87-THR95 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1q3q |
Chain | Residue | Details |
A | THR97 | |
A | ASP390 | |
A | THR96 | |
A | ASP63 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1q3q |
Chain | Residue | Details |
B | ASP391 | |
B | THR95 | |
B | ASP62 | |
B | THR96 | |