2VW5
Structure Of The Hsp90 Inhibitor 7-O-carbamoylpremacbecin Bound To The N- Terminus Of Yeast Hsp90
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BC6 A 500 |
| Chain | Residue |
| A | ASN37 |
| A | GLY121 |
| A | VAL122 |
| A | GLY123 |
| A | PHE124 |
| A | THR171 |
| A | HOH2055 |
| A | HOH2113 |
| A | HOH2114 |
| A | ASP40 |
| A | ALA41 |
| A | LYS44 |
| A | ASP79 |
| A | ILE82 |
| A | ASN92 |
| A | LEU93 |
| A | LYS98 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BC6 B 500 |
| Chain | Residue |
| B | ASN37 |
| B | ASP40 |
| B | ALA41 |
| B | ASP79 |
| B | ILE82 |
| B | GLU88 |
| B | ASN92 |
| B | LEU93 |
| B | GLY121 |
| B | VAL122 |
| B | GLY123 |
| B | PHE124 |
| B | THR171 |
| B | HOH2028 |
| B | HOH2062 |
| B | HOH2124 |
| B | HOH2125 |
| B | HOH2126 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BC6 C 500 |
| Chain | Residue |
| C | ASN37 |
| C | ASP40 |
| C | ALA41 |
| C | LYS44 |
| C | ASP79 |
| C | ILE82 |
| C | ASN92 |
| C | LEU93 |
| C | GLY121 |
| C | VAL122 |
| C | GLY123 |
| C | PHE124 |
| C | THR171 |
| C | HOH2018 |
| C | HOH2050 |
| C | HOH2107 |
| C | HOH2108 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BC6 D 500 |
| Chain | Residue |
| D | ASN37 |
| D | ASP40 |
| D | ALA41 |
| D | LYS44 |
| D | ASP79 |
| D | ILE82 |
| D | ASN92 |
| D | LEU93 |
| D | GLY121 |
| D | VAL122 |
| D | GLY123 |
| D | PHE124 |
| D | THR171 |
| D | HOH2035 |
| D | HOH2096 |
| D | HOH2097 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A1215 |
| Chain | Residue |
| A | ARG65 |
| A | ARG78 |
| A | GLU165 |
| A | HOH2115 |
| D | LYS69 |
| D | GLN72 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C1215 |
| Chain | Residue |
| B | LYS69 |
| B | GLN72 |
| C | ARG78 |
| C | GLU165 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D1215 |
| Chain | Residue |
| A | LYS69 |
| A | GLN72 |
| A | HOH2048 |
| D | ARG65 |
| D | ARG78 |
| D | GLU165 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C1216 |
| Chain | Residue |
| C | LYS98 |
| C | SER99 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B1215 |
| Chain | Residue |
| B | ARG65 |
| B | ARG78 |
| B | GLU165 |
| C | LYS69 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A1216 |
| Chain | Residue |
| A | LYS98 |
| A | SER99 |
| D | LYS102 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D1216 |
| Chain | Residue |
| A | LYS102 |
| D | LYS98 |
| D | SER99 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B1216 |
| Chain | Residue |
| C | LYS102 |
| B | LYS98 |
| B | SER99 |
| B | HOH2069 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A1217 |
| Chain | Residue |
| A | GLU149 |
| A | ASN151 |
| A | SER155 |
| A | PHE156 |
| A | THR157 |
| A | HOH2084 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9230303","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AM1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1AMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WEP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
