{"resolution": "", "ligand_mw": "105.09", "secondary_structure": "MAPRGFSCLLLLTSEIDLPVKRRA#CCCSSHHHHHHHHTTTCSTTTCCC", "inchi": "InChI=1S/C3H7NO3/c4-2(1-5)3(6)7/h2,5H,1,4H2,(H,6,7)/t2-/m1/s1", "method": "SOLUTION NMR", "ec_number": "", "uniprot_ac": "Q8IVG9", "remarks": "Solution NMR structure of Humanin containing a D-isomerized serine residue", "description": "They demonstrated that Humanin d-Ser14 exhibited potent inhibitory activity against fibrillation of amyloid-Beta and remarkably higher binding affinity for amyloid-Beta than that of the Humanin wild-type and S14G mutant. The solution structure of Humanin d-Ser14 showed that d-isomerization of the Ser14 residue enables drastic conformational rearrangement of Humanin. Furthermore, they identified an amyloid-Beta-binding site on Humanin d-Ser14.", "type": "Inhibitor complex", "ligand_smiles": "C([C@H](C(=O)O)N)O", "chain_id": "X", "species": "Homo sapiens", "keyword": "Humanin", "ligstr": "DSN:X:C3 H7 N O3:105.09:D-SERINE:C([C@H](C(=O)O)N)O:InChI=1S/C3H7NO3/c4-2(1-5)3(6)7/h2,5H,1,4H2,(H,6,7)/t2-/m1/s1:MTCFGRXMJLQNBG-UWTATZPHSA-N", "pmid": "27349871", "mutation_s_field": "D-isomerized serine ", "author": "Alsanousi, N., Sugiki, T., Furuita, K., So, M., Lee, Y.H., Fujiwara, T., Kojima, C.", "pdb_id": "5GIW", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "MTCFGRXMJLQNBG-UWTATZPHSA-N", "ligand_name": "D-SERINE", "ligand_formula": "C3 H7 N O3", "ligand_id": "DSN", "r_value_free": "", "protein_name": "Humanin", "gene_names": "MT-RNR2, HN", "global_stoichiometry": "Monomer - A", "alternative_name": "Humanin mitochondrial", "peptide_protein_sequence": "chain-ID X: MAPRGFSCLLLLTSEIDLPVKRRA", "pdb_classification": "APOPTOSIS", "reference": "Biochem Biophys Res Commun. 2016 Sep 2;477(4):647-653.", "length": "24", "entry": "S-0428"}