5J8U
Crystal Structure of Hsp90-alpha N-domain L107A mutant in complex with 5-(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 | 13 |
Details | binding site for residue 6DL A 301 |
Chain | Residue |
A | LEU48 |
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 | 13 |
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 | THR184 |
B | VAL186 |
B | HOH411 |
B | HOH445 |
B | HOH521 |
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 |