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 | 18 |
Details | BINDING SITE FOR RESIDUE N5O A 401 |
Chain | Residue |
A | ASN107 |
A | THR245 |
A | HOH510 |
A | HOH521 |
A | HOH529 |
A | HOH538 |
A | HOH549 |
A | HOH550 |
A | HOH552 |
A | HOH559 |
A | ALA111 |
A | ASP149 |
A | MET154 |
A | ASN162 |
A | LEU163 |
A | GLY196 |
A | VAL197 |
A | TYR200 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PG4 A 501 |
Chain | Residue |
A | THR212 |
A | ARG237 |
A | THR240 |
A | THR246 |
A | THR248 |
A | PG4502 |
A | HOH512 |
A | HOH513 |
A | HOH514 |
A | HOH551 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 A 502 |
Chain | Residue |
A | LYS137 |
A | HIS146 |
A | TRP282 |
A | PG4501 |
A | HOH517 |
A | HOH530 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 A 505 |
Chain | Residue |
A | ASP110 |
A | LYS114 |
A | LEU117 |
A | HOH598 |
A | HOH611 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 A 508 |
Chain | Residue |
A | LYS75 |
A | PHE76 |
A | ALA77 |
A | HOH515 |
A | HOH620 |
B | HOH811 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 701 |
Chain | Residue |
B | ASP218 |
B | HOH702 |
B | HOH704 |
B | HOH705 |
B | HOH706 |
B | HOH707 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE N5O B 402 |
Chain | Residue |
B | ALA111 |
B | ASP149 |
B | MET154 |
B | ASN162 |
B | LEU163 |
B | GLY196 |
B | PHE199 |
B | TYR200 |
B | THR245 |
B | HOH710 |
B | HOH735 |
B | HOH740 |
B | HOH749 |
B | HOH755 |
B | HOH762 |
B | HOH764 |
B | HOH766 |
B | HOH809 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PG4 B 503 |
Chain | Residue |
B | THR212 |
B | ARG237 |
B | THR240 |
B | THR246 |
B | THR248 |
B | HOH708 |
B | HOH747 |
B | HOH801 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 B 504 |
Chain | Residue |
B | LYS137 |
B | TRP282 |
B | HOH773 |
B | HOH803 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 B 506 |
Chain | Residue |
B | GLU130 |
B | ASN239 |
B | GLY242 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG4 B 507 |
Chain | Residue |
B | ASP262 |
B | THR263 |
B | ASN266 |
B | HOH720 |
B | HOH805 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1PE B 601 |
Chain | Residue |
B | HOH741 |
A | ASN83 |
A | MET86 |
A | LYS87 |
A | ILE90 |
A | SER227 |
B | ASN83 |
B | LYS87 |
B | ILE90 |
B | SER227 |
B | HOH715 |
Functional Information from PROSITE/UniProt
site_id | PS00298 |
Number of Residues | 10 |
Details | HSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE |
Chain | Residue | Details |
A | TYR94-GLU103 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASN107 | |
B | ASN107 | |
Chain | Residue | Details |
A | ASP149 | |
A | PHE199 | |
B | ASP149 | |
B | PHE199 | |
Chain | Residue | Details |
A | ASN162 | |
B | ASN162 | |
Chain | Residue | Details |
A | LYS168 | |
B | LYS168 | |
Chain | Residue | Details |
A | SER172 | |
B | SER172 | |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN107 | |
A | ASN217 | |
B | ASN107 | |
B | ASN217 | |