{"resolution": "1.16", "ligand_mw": "40.08%%112.41%%78.13%%131.17", "secondary_structure": "ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK#CCCEEEEEEEECTTSCEEEEEEEESSSEESEETTSTTCEEEEECTTSSSSSCEECEESSSEECSGGGHHHHHHHHHHHHHHHHHHHHHCCCSTTSSCCCEEEEEEESSSCCCEEECSSCEEEECCCSSSBSCGGGCHHHHHHHHHHHHHHHTTCCCSSHHHHHHHHHHHHHHHHHHHHHHTSSCCSEESTTTBCTTSTTCCSEESSCGGGGTCCSSGGGCCCSSHHHHHTTTTHHHHHHHHHHHHHCEEETTEEECCCCHHHHHHHHHHHHHHTCCTTCCHHHHHHHHHHHHHHHHCTTSHHHHHHHHHHHHTTCC", "inchi": "InChI=1S/Ca/q+2%%InChI=1S/Cd/q+2%%InChI=1S/C2H6OS/c1-4(2)3/h1-2H3%%InChI=1S/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1", "method": "X-RAY DIFFRACTION", "ec_number": "3.4.24.27", "uniprot_ac": "P43133", "remarks": "Alzheimer's Amyloid-Beta Peptide Fragment 31-35 in Complex with Cd-substituted Thermolysin", "description": "The interaction of the amyloid-Beta peptide (ABeta) with thermolysin (TLN) was investigated by X-ray crystallography. Structural models of the complexes of TLN with several ABeta fragments show that, despite the numerous possible cleavage sites of the ABeta sequence, the C-terminal product of Ala30-Ile31 cleavage does not dissociate, thus inhibiting the enzyme. The high similarity between the TLN structural motif and neprilysin (NEP), the most extensively studied peptidase associated with ABeta clearance, suggests that NEP should be more efficient against ABeta polymorphs where Ala30-Ile31 is inaccessible.", "type": "Inhibitor complex", "ligand_smiles": "[Ca+2]%%[Cd+2]%%CS(=O)C%%CC[C@H](C)[C@@H](C(=O)O)N", "chain_id": "A%%A%%A%%A", "species": "Geobacillus stearothermophilus", "keyword": "Thermolysin", "ligstr": "CA:A:Ca 2:40.08:CALCIUM ION:[Ca+2]:InChI=1S/Ca/q+2:BHPQYMZQTOCNFJ-UHFFFAOYSA-N;CD:A:Cd 2:112.41:CADMIUM ION:[Cd+2]:InChI=1S/Cd/q+2:WLZRMCYVCSSEQC-UHFFFAOYSA-N;DMS:A:C2 H6 O S:78.13:DIMETHYL SULFOXIDE:CS(=O)C:InChI=1S/C2H6OS/c1-4(2)3/h1-2H3:IAZDPXIOMUYVGZ-UHFFFAOYSA-N;ILE:A:C6 H13 N O2:131.17:ISOLEUCINE:CC[C@H](C)[C@@H](C(=O)O)N:InChI=1S/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1:AGPKZVBTJJNPAG-WHFBIAKZSA-N", "pmid": "30403288", "mutation_s_field": "No", "author": "Leite, J.P., Gales, L.", "pdb_id": "6GHX", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "BHPQYMZQTOCNFJ-UHFFFAOYSA-N%%WLZRMCYVCSSEQC-UHFFFAOYSA-N%%IAZDPXIOMUYVGZ-UHFFFAOYSA-N%%AGPKZVBTJJNPAG-WHFBIAKZSA-N", "ligand_name": "CALCIUM ION%%CADMIUM ION%%DIMETHYL SULFOXIDE%%ISOLEUCINE", "ligand_formula": "Ca 2%%Cd 2%%C2 H6 O S%%C6 H13 N O2", "ligand_id": "CA%%CD%%DMS%%ILE", "r_value_free": "0.22", "protein_name": "Thermolysin", "gene_names": "nprS, nprM", "global_stoichiometry": "Monomer - A", "alternative_name": "Neutral protease", "peptide_protein_sequence": "chain-ID A: ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK", "pdb_classification": "HYDROLASE", "reference": "FEBS Lett. 2019 Jan;593(1):128-137.", "length": "316", "entry": "S-0549"}