{"resolution": "1.9", "ligand_mw": "96.06", "secondary_structure": "MGGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADS#CCCCEEEEEESSCBCCSSTTBCCBCTTCEEEEETTCCSSEEEEEETTTCCEEEEEGGGEEECCC", "inchi": "InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2", "method": "X-RAY DIFFRACTION", "ec_number": "2.7.10.2", "uniprot_ac": "P07947", "remarks": "Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: Loop flexibility and amyloid aggregation.", "description": "high-resolution crystal structure of the SH3 domain of the c-Yes oncogen. Comparison with other SH3 domains from the Src family revealed significant deviations in the loop regions. In particular, the n-Src loop, highly flexible and partially disordered, is stabilized in an unusual conformation by the establishment of several intramolecular hydrogen bonds. Additionally, it is the first report of amyloid aggregation by an SH3 domain from the Src family.", "type": "Protein", "ligand_smiles": "[O-]S(=O)(=O)[O-]", "chain_id": "A", "species": "Homo sapiens", "keyword": "Proto-oncogene tyrosine-protein kinase Yes", "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", "pmid": "17418139", "mutation_s_field": "No", "author": "Martin-Garcia, J.M., Luque, I., Mateo, P.L., Ruiz-Sanz, J., Camara-Artigas, A.", "pdb_id": "2HDA", "amyloid_non_amyloid": "Amyloid", "inchi_key": "QAOWNCQODCNURD-UHFFFAOYSA-L", "ligand_name": "SULFATE ION", "ligand_formula": "O4 S -2", "ligand_id": "SO4", "r_value_free": "0.27", "protein_name": "Tyrosine-protein kinase Yes", "gene_names": "YES1, YES", "global_stoichiometry": "Monomer - A ", "alternative_name": "Proto-oncogene c-Yes, p61-Yes", "peptide_protein_sequence": "chain-ID A: MGGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADS", "pdb_classification": "TRANSFERASE", "reference": "FEBS Lett. 2007 May 1;581(9):1701-6. Epub  2007 Mar 30", "length": "64", "entry": "S-0111"}