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 | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
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 | 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 |
C | 0005524 | molecular_function | ATP binding |
C | 0006457 | biological_process | protein folding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
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 | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
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 | 22 |
Details | binding site for residue ANP A 601 |
Chain | Residue |
A | SER34 |
A | THR89 |
A | THR90 |
A | THR91 |
A | ILE152 |
A | ARG155 |
A | ASP373 |
A | GLY389 |
A | GLY390 |
A | MET430 |
A | PHE461 |
A | LEU35 |
A | MET469 |
A | ASP476 |
A | MG602 |
A | GLY36 |
A | PRO37 |
A | ASN55 |
A | ASP56 |
A | GLY57 |
A | ASP87 |
A | GLY88 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue MG A 602 |
Chain | Residue |
A | ASP87 |
A | ANP601 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue ANP B 601 |
Chain | Residue |
B | SER34 |
B | LEU35 |
B | GLY36 |
B | PRO37 |
B | ASN55 |
B | ASP56 |
B | GLY57 |
B | ASP87 |
B | GLY88 |
B | THR89 |
B | THR90 |
B | THR91 |
B | ILE152 |
B | ARG155 |
B | ASP373 |
B | GLY389 |
B | GLY390 |
B | MET430 |
B | PHE461 |
B | VAL474 |
B | ASP476 |
B | MG602 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue MG B 602 |
Chain | Residue |
B | ASP87 |
B | ANP601 |
site_id | AC5 |
Number of Residues | 20 |
Details | binding site for residue ANP C 601 |
Chain | Residue |
C | SER34 |
C | LEU35 |
C | GLY36 |
C | ASN55 |
C | ASP56 |
C | GLY57 |
C | ASP87 |
C | GLY88 |
C | THR89 |
C | THR90 |
C | THR91 |
C | ILE152 |
C | ARG155 |
C | ASP373 |
C | GLY389 |
C | GLY390 |
C | MET430 |
C | PHE461 |
C | ASP476 |
C | MG602 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MG C 602 |
Chain | Residue |
C | ASP87 |
C | ASP373 |
C | ANP601 |
site_id | AC7 |
Number of Residues | 22 |
Details | binding site for residue ANP D 601 |
Chain | Residue |
D | SER34 |
D | LEU35 |
D | GLY36 |
D | PRO37 |
D | ASN55 |
D | ASP56 |
D | GLY57 |
D | ASP87 |
D | GLY88 |
D | THR89 |
D | THR90 |
D | THR91 |
D | ILE152 |
D | ARG155 |
D | ASP373 |
D | GLY389 |
D | GLY390 |
D | MET430 |
D | PHE461 |
D | VAL474 |
D | ASP476 |
D | MG602 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue MG D 602 |
Chain | Residue |
D | ASP87 |
D | ANP601 |
Functional Information from PROSITE/UniProt
site_id | PS00995 |
Number of Residues | 9 |
Details | TCP1_3 Chaperonins TCP-1 signature 3. QEreVGDGT |
Chain | Residue | Details |
A | GLN81-THR89 | |