5J8M
Crystal Structure of Hsp90-alpha N-domain L107A mutant in complex with 5-(5-Bromo-2,4-dihydroxy-phenyl)-4-(2-fluoro-phenyl)-2,4-dihydro-[1,2,4]triazol-3-one
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 | 14 |
| Details | binding site for residue 6DL A 301 |
| Chain | Residue |
| A | LEU48 |
| A | PHE138 |
| A | THR184 |
| A | VAL186 |
| A | HOH403 |
| A | HOH404 |
| A | ASN51 |
| A | ALA55 |
| A | LYS58 |
| A | ASP93 |
| A | ILE96 |
| A | GLY97 |
| A | MET98 |
| A | GLY108 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 6DL B 301 |
| Chain | Residue |
| B | ASN51 |
| B | ALA55 |
| B | LYS58 |
| B | ASP93 |
| B | ILE96 |
| B | GLY97 |
| B | MET98 |
| B | ASN106 |
| B | PHE138 |
| B | THR184 |
| B | VAL186 |
| B | HOH418 |
| B | HOH451 |
| B | HOH537 |
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 | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU16 | |
| B | GLU16 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 | THR109 | |
| B | THR109 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | MET130 | |
| B | MET130 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | ALA141 | |
| B | ALA141 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07901 |
| Chain | Residue | Details |
| A | LYS191 | |
| B | LYS191 |
