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Ligands
Code Name Style Show Link
CL Chloride ion
012 (4s)-N-[(1s,2r)-1-benzyl-3-{[3-(dimethylamino)benzyl]amino}-2-hydroxypropyl]-1-(3-methoxybenzyl)-2-oxoimidazolidine-4-carboxamide
Non-standard Residues
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Code : 3CKP   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of BACE-1 in complex with inhibitor
Release Data : 2008-06-03
Compound :
mol_id molecule chains synonym
1 Beta-secretase 1 A,B,C Beta-site APP cleaving enzyme 1, Beta-site amyloid precursor protein cleaving enzyme 1, Membrane-associated aspartic protease 2, Memapsin-2, Aspartyl protease 2, Asp 2, ASP2
ec: 3.4.23.46
fragment: protease domain, UNP residues 43-454
mutation: R-6K, R-6K
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens Human Escherichia coli
Authors : Min, K.
Keywords : beta-secretase, aspartyl protease, Alternative splicing, Glycoprotein, Hydrolase, Membrane, Transmembrane, Zymogen
Exp. method : X-RAY DIFFRACTION ( 2.300 Å )
Citation :

Synthesis, SAR, and X-ray structure of human BACE-1 inhibitors with cyclic urea derivatives

Park, H.,Min, K.,Kwak, H.-S.  et al.
(2008)  Bioorg.Med.Chem.Lett.  18 : 2900 - 2904

PubMed: 18434152
DOI: 10.1016/j.bmcl.2008.03.081

Chain : A, B, C
UniProt : P56817 (BACE1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|- Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein. 3.4.23.46 PubMed:10677483
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