1UYL
Structure-Activity Relationships in purine-based inhibitor binding to HSP90 isoforms
Functional Information from GO Data
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 | TYR38-GLU47 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | SER52 | |
A | THR94 | |
A | TYR139 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER113 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:2507541 |
Chain | Residue | Details |
A | GLN6 | |
A | GLN8 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901 |
Chain | Residue | Details |
A | ILE59 | |
A | GLN85 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | ASP232 |