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 | 0051087 | molecular_function | protein-folding chaperone binding |
| D | 0051087 | molecular_function | protein-folding chaperone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP A 1211 |
| Chain | Residue |
| A | ASN39 |
| A | PHE126 |
| A | THR173 |
| A | MET175 |
| A | MG1212 |
| A | HOH2031 |
| A | HOH2078 |
| A | HOH2079 |
| A | HOH2080 |
| A | HOH2081 |
| A | HOH2082 |
| A | ALA43 |
| E | HIS188 |
| A | ASP81 |
| A | MET86 |
| A | ASN94 |
| A | LEU95 |
| A | GLY123 |
| A | VAL124 |
| A | GLY125 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1212 |
| Chain | Residue |
| A | ASN39 |
| A | ADP1211 |
| A | HOH2016 |
| A | HOH2020 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP B 1211 |
| Chain | Residue |
| B | ASN39 |
| B | ALA43 |
| B | ASP81 |
| B | MET86 |
| B | ASN94 |
| B | GLY123 |
| B | VAL124 |
| B | GLY125 |
| B | PHE126 |
| B | THR173 |
| B | MET175 |
| B | MG1212 |
| B | HOH2013 |
| B | HOH2027 |
| B | HOH2069 |
| B | HOH2070 |
| B | HOH2071 |
| F | HIS188 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1212 |
| Chain | Residue |
| B | ASN39 |
| B | ADP1211 |
| B | HOH2008 |
| F | ASP189 |
| F | HOH2023 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 1222 |
| Chain | Residue |
| E | CYS159 |
| E | CYS164 |
| E | CYS178 |
| E | HIS218 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 1223 |
| Chain | Residue |
| E | HIS181 |
| E | CYS196 |
| E | CYS197 |
| E | CYS213 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 1222 |
| Chain | Residue |
| F | CYS159 |
| F | CYS164 |
| F | CYS178 |
| F | HIS218 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 1223 |
| Chain | Residue |
| F | HIS181 |
| F | CYS196 |
| F | CYS197 |
| F | CYS213 |
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 | TYR26-GLU35 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI4 |
| Number of Residues | 118 |
| Details | Domain: {"description":"CHORD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00734","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20670895","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XCM","evidenceCode":"ECO:0007744"}]} |
