{"reference": "PLoS One. 2014 Dec 9;9(12):e113224.", "alternative_name": "Proto-oncogene c-Src, pp60c-src", "entry": "S-0334", "gene_names": "SRC", "remarks": "Crystal structure of the chicken c-Src-SH3 domain intertwined dimer", "secondary_structure": "GSHMTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSD#CCCCEEECSSCBCCCSSSSCCBCTTCEEECCCCTTCSEEEEECTTTCCEEEEEGGGCCCCC", "chain_id": "A%%A", "inchi": "InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2%%InChI=1S/C6H14O4/c7-1-3-9-5-6-10-4-2-8/h7-8H,1-6H2", "amyloid_non_amyloid": "Amyloid", "pmid": "25490095", "ligand_smiles": "C(COCCO)O%%C(COCCOCCO)O", "keyword": "Proto-oncogene tyrosine-protein kinase Src", "peptide_protein_sequence": "chain-ID A: GSHMTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSD", "uniprot_ac": "P00523", "protein_name": "Proto-oncogene tyrosine-protein kinase Src", "r_value_free": "0.24100000", "mutation_s_field": "No", "ligand_mw": "106.12%%150.17", "pdb_id": "4JZ3", "inchi_key": "MTHSVFCYNBDYFN-UHFFFAOYSA-N%%ZIBGPFATKBEMQZ-UHFFFAOYSA-N", "ec_number": "2.7.10.2", "pdb_classification": "SIGNALING PROTEIN", "type": "Protein", "author": "Bacarizo, J., Martinez-Rodriguez, S., Martin-Garcia, J.M., Andujar-Sanchez, M., Ortiz-Salmeron, E., Neira, J.L., Camara-Artigas, A.", "species": "Gallus gallus", "ligand_id": "PEG%%PGE", "method": "X-RAY DIFFRACTION", "ligand_name": "DI(HYDROXYETHYL)ETHER%%TRIETHYLENE GLYCOL", "global_stoichiometry": "Monomer - A ", "resolution": "1.85", "ligand_formula": "C4 H10 O3%%C6 H14 O4", "length": "61", "ligstr": "PEG:A:C4 H10 O3:106.12:DI(HYDROXYETHYL)ETHER:C(COCCO)O:InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2:MTHSVFCYNBDYFN-UHFFFAOYSA-N;PGE:A:C6 H14 O4:150.17:TRIETHYLENE GLYCOL:C(COCCOCCO)O:InChI=1S/C6H14O4/c7-1-3-9-5-6-10-4-2-8/h7-8H,1-6H2:ZIBGPFATKBEMQZ-UHFFFAOYSA-N", "description": "They have solved the crystallographic structures of the wild-type (WT) and Gln128Glu, Gln128Lys and Gln128Arg mutants from crystals obtained at different pHs. At pH 5.0, crystals belong to the hexagonal space group P6?22 and the asymmetric unit is formed by one chain of the protomer of the c-Src-SH3 domain in an open conformation. At pH 7.0, crystals belong to the orthorhombic space group P2?2?2?, with two molecules at the asymmetric unit showing the characteristic fold of the SH3 domain. The residue at position 128 is connected to Glu106 at the diverging Beta-turn through a cluster of water molecules."}