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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 2GJ A 301 |
Chain | Residue |
A | ASN37 |
A | GLY121 |
A | PHE124 |
A | THR171 |
A | MET173 |
A | SER38 |
A | ALA41 |
A | ASP79 |
A | ILE82 |
A | GLY83 |
A | MET84 |
A | ASP88 |
A | ASN92 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue 2GJ B 301 |
Chain | Residue |
B | ASN37 |
B | SER38 |
B | ALA41 |
B | ASP79 |
B | ILE82 |
B | GLY83 |
B | MET84 |
B | ASN92 |
B | GLY121 |
B | PHE124 |
B | THR171 |
B | MET173 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue 2GJ C 301 |
Chain | Residue |
C | LEU34 |
C | ASN37 |
C | SER38 |
C | ALA41 |
C | ASP79 |
C | ILE82 |
C | GLY83 |
C | MET84 |
C | ASN92 |
C | LEU93 |
C | GLY121 |
C | PHE124 |
C | THR171 |
C | MET173 |
E | ASP142 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue 2GJ D 301 |
Chain | Residue |
D | LEU34 |
D | ASN37 |
D | SER38 |
D | ASP40 |
D | ALA41 |
D | LYS44 |
D | ASP79 |
D | GLY83 |
D | MET84 |
D | ASP88 |
D | ASN92 |
D | LEU93 |
D | GLY121 |
D | PHE124 |
D | THR171 |
D | MET173 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue 2GJ E 301 |
Chain | Residue |
A | TYR47 |
E | LEU34 |
E | ASN37 |
E | SER38 |
E | ALA41 |
E | LYS44 |
E | ASP79 |
E | ILE82 |
E | GLY83 |
E | MET84 |
E | GLY121 |
E | PHE124 |
E | THR171 |
E | MET173 |
site_id | AC6 |
Number of Residues | 14 |
Details | binding site for residue 2GJ F 301 |
Chain | Residue |
F | LEU34 |
F | ASN37 |
F | ALA41 |
F | LYS44 |
F | ASP79 |
F | GLY83 |
F | MET84 |
F | ASP88 |
F | ASN92 |
F | LEU93 |
F | GLY121 |
F | PHE124 |
F | THR171 |
F | MET173 |
Functional Information from PROSITE/UniProt
site_id | PS00298 |
Number of Residues | 10 |
Details | HSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE |
Chain | Residue | Details |
A | TYR24-GLU33 | |