{"global_stoichiometry": "Homo 4-mer - A4 ", "ligstr": "CL:A:Cl -1:35.45:CHLORIDE ION:[Cl-]:InChI=1S/ClH/h1H/p-1:VEXZGXHMUGYJMC-UHFFFAOYSA-M;nan:A:Na 1:22.99:SODIUM ION:[Na+]:InChI=1S/Na/q+1:FKNQFGJONOIPTF-UHFFFAOYSA-N", "uniprot_ac": "Q99714", "inchi": "InChI=1S/ClH/h1H/p-1%%InChI=1S/Na/q+1", "reference": "Science. 2004 Apr 16;304(5669):448-52", "author": "Lustbader, J.W., Cirilli, M., Lin, C., Xu, H.W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., Trinchese, F., Gunn-Moore, F., Lue, L.F., Walker, D.G., Kuppusamy, P., Zewier, Z.L., Arancio, O., Stern, D., Yan, S.S., Wu, H.", "type": "Protein complex", "ligand_id": "CL%%nan", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "3-hydroxyacyl-CoA dehydrogenase type II", "gene_names": "HSD17B10, ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2", "chain_id": "A%%A", "ligand_mw": "35.45%%22.99", "inchi_key": "VEXZGXHMUGYJMC-UHFFFAOYSA-M%%FKNQFGJONOIPTF-UHFFFAOYSA-N", "secondary_structure": "MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP#CCCCCCCCTTCEEEEETTTSHHHHHHHHHHHHTTCEEEEEECTTSSHHHHHHHTCTTEEEEECCTTCHHHHHHHHHHHHHHHSCCCEEECCTTCCCCCCCCCCCCCCCCCCCCCCSSSCHHHHHHHHHHHHHHHHHHTSCCCTTCCCEEEEEECCBCCCCCCCSGGGGCCBCSHHHHHHHHHHHHHGGGTEEEEEEECCSSCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHCTTCCSCEEECCCCCCCCC", "amyloid_non_amyloid": "Amyloid", "length": "261", "remarks": "Abeta-bound human ABAD structure", "protein_name": "3-hydroxyacyl-CoA dehydrogenase type-2", "peptide_protein_sequence": "chain-ID A: MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP", "ligand_name": "CHLORIDE ION%%SODIUM ION", "ligand_smiles": "[Cl-]%%[Na+]", "pdb_id": "1SO8", "ec_number": "1.1.1.35", "pdb_classification": "OXIDOREDUCTASE", "mutation_s_field": "No", "ligand_formula": "Cl -1%%Na 1", "r_value_free": "0.261", "alternative_name": "17-beta-hydroxysteroid dehydrogenase 10, 2-methyl-3-hydroxybutyryl-CoA dehydrogenase, 3-hydroxy-2-methylbutyryl-CoA dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase type II, Endoplasmic reticulum-associated amyloid beta-peptide-binding protein, Mitochondria", "description": "Demonstrated that ABeta-binding alcohol dehydrogenase (ABAD) is a direct molecular link from ABeta to mitochondrial toxicity. ABeta interacts with ABAD in the mitochondria of AD patients and transgenic mice. The crystal structure of ABeta-bound ABAD shows substantial deformation of the active site that prevents nicotinamide adenine dinucleotide (NAD) binding. An ABAD peptide specifically inhibits ABAD-ABeta interaction and suppresses ABeta-induced apoptosis and free-radical generation in neurons. ", "resolution": "2.3", "pmid": "15087549", "entry": "S-0063"}