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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 2000 |
| Chain | Residue |
| A | ASN38 |
| A | ADP1000 |
| A | HOH3001 |
| A | HOH3002 |
| A | HOH3003 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP A 1000 |
| Chain | Residue |
| A | HIS93 |
| A | LYS99 |
| A | LYS103 |
| A | GLY126 |
| A | PHE127 |
| A | THR174 |
| A | MG2000 |
| A | HOH3001 |
| A | HOH3002 |
| A | HOH3003 |
| A | HOH3004 |
| A | HOH3006 |
| A | HOH3007 |
| A | HOH3009 |
| A | HOH3067 |
| A | HOH3101 |
| A | HOH3134 |
| A | HOH3212 |
| A | HOH3214 |
| A | ASN38 |
| A | ALA42 |
| A | ASP80 |
| A | MET85 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HEZ A 4000 |
| Chain | Residue |
| A | PHE9 |
| A | LYS14 |
| A | ASP44 |
| A | ARG47 |
| A | PHE48 |
| A | LEU51 |
| A | GLN122 |
| A | HOH3024 |
| A | HOH3042 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HEZ A 4001 |
| Chain | Residue |
| A | GLN10 |
| A | ARG33 |
| A | GLU34 |
| A | SER37 |
| A | GLY121 |
| A | GLY124 |
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 | TYR25-GLU34 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15837196","evidenceCode":"ECO:0000269"}]} |
