{"resolution": "1.6", "ligand_mw": "96.06%%96.06", "secondary_structure": "MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEVEKVDESFSEYKGEFEDFETY#CCCCCCCCCCCCEEEEEEEEEEECSSSSHHHHHHHHHHHHTCEEEEEECTTSCEEEEEEEEHHHHHHHHHHHHHCSTTCEEEEEEEEEECCCCCCSSEEEC&MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEVEKVDESFSEYKGEFEDFETY#CCCCCCCCCCCCEEEEEEEEEEECSSSSHHHHHHHHHHHHTCEEEEEECTTSCEEEEEEEEHHHHHHHHHHHHHCSTTCEEEEEEEEEECCCCCCCSEEEC", "inchi": "InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2%%InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2", "method": "X-RAY DIFFRACTION", "ec_number": "3.6.1.7", "uniprot_ac": "Q97ZL0", "remarks": "The crystal structure of truncated, Y86E mutant of S. solfataricus acylphosphatase", "description": "Three single Sso AcP mutants (V84D, Y86E and V84P) were designed to engineer additional protection against aggregation in B4 and were observed to successfully impair native-like aggregation in all three variants at the expense of a lower stability. To understand the structural basis of the reduced aggregation propensity and lower stability, the crystal structures of the Sso AcP variants were determined in the present study. Structural analysis reveals that the V84D and Y86E mutations exert protection by the insertion of an edge negative charge. A conformationally less regular B4 underlies protection against aggregation in the V84P mutant.", "type": "Protein", "ligand_smiles": "[O-]S(=O)(=O)[O-]%%[O-]S(=O)(=O)[O-]", "chain_id": "A%%B", "species": "Saccharolobus solfataricus", "keyword": "Acylphosphatase", "ligstr": "SO4:A:O4 S -2:96.06:SULFATE ION:[O-]S(=O)(=O)[O-]:InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2:QAOWNCQODCNURD-UHFFFAOYSA-L;SO4:B:O4 S -2:96.06:SULFATE ION:[O-]S(=O)(=O)[O-]:InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2:QAOWNCQODCNURD-UHFFFAOYSA-L", "pmid": "24893801", "mutation_s_field": "[del]N11/Y86E", "author": "de Rosa, M., Bemporad, F., Pellegrino, S., Chiti, F., Bolognesi, M., Ricagno, S.", "pdb_id": "4OJH", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "QAOWNCQODCNURD-UHFFFAOYSA-L%%QAOWNCQODCNURD-UHFFFAOYSA-L", "ligand_name": "SULFATE ION%%SULFATE ION", "ligand_formula": "O4 S -2%%O4 S -2", "ligand_id": "SO4%%SO4", "r_value_free": "0.23800000", "protein_name": "Acylphosphatase", "gene_names": "acyP, SSO0887", "global_stoichiometry": "Monomer - A ", "alternative_name": "Acylphosphate phosphohydrolase", "peptide_protein_sequence": "chain-ID A: MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEVEKVDESFSEYKGEFEDFETY; chain-ID B: MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEVEKVDESFSEYKGEFEDFETY", "pdb_classification": "HYDROLASE", "reference": "FEBS J. 2014 Sep;281(18):4072-84.", "length": "101", "entry": "S-0357"}