Entry Database : PDB / ID : 4bfd Structure visualization Downloads & linksTitle CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH CHEMICAL LIGAND ComponentsBETA-SECRETASE 1 Details Keywords HYDROLASEFunction / homology Function and homology informationFunction Domain/homology Component
memapsin 2 / Golgi-associated vesicle lumen / beta-aspartyl-peptidase activity / signaling receptor ligand precursor processing / amyloid-beta formation / amyloid precursor protein catabolic process / membrane protein ectodomain proteolysis / cellular response to manganese ion / amyloid-beta metabolic process / detection of mechanical stimulus involved in sensory perception of pain ... memapsin 2 / Golgi-associated vesicle lumen / beta-aspartyl-peptidase activity / signaling receptor ligand precursor processing / amyloid-beta formation / amyloid precursor protein catabolic process / membrane protein ectodomain proteolysis / cellular response to manganese ion / amyloid-beta metabolic process / detection of mechanical stimulus involved in sensory perception of pain / prepulse inhibition / cellular response to copper ion / multivesicular body / presynaptic modulation of chemical synaptic transmission / protein serine/threonine kinase binding / hippocampal mossy fiber to CA3 synapse / trans-Golgi network / response to lead ion / recycling endosome / protein processing / cellular response to amyloid-beta / positive regulation of neuron apoptotic process / late endosome / synaptic vesicle / peptidase activity / amyloid-beta binding / endopeptidase activity / amyloid fibril formation / aspartic-type endopeptidase activity / early endosome / lysosome / endosome / endosome membrane / membrane raft / endoplasmic reticulum lumen / Amyloid fiber formation / axon / neuronal cell body / dendrite / enzyme binding / cell surface / Golgi apparatus / proteolysis / membrane / plasma membrane Similarity search - Function Beta-secretase BACE1 / Beta-secretase BACE / Memapsin-like / Eukaryotic aspartyl protease / Aspartic peptidase A1 family / Peptidase family A1 domain / Peptidase family A1 domain profile. / Cathepsin D, subunit A; domain 1 / Acid Proteases / Aspartic peptidase, active site ... Beta-secretase BACE1 / Beta-secretase BACE / Memapsin-like / Eukaryotic aspartyl protease / Aspartic peptidase A1 family / Peptidase family A1 domain / Peptidase family A1 domain profile. / Cathepsin D, subunit A; domain 1 / Acid Proteases / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Beta Barrel / Mainly Beta Similarity search - Domain/homologyBiological species HOMO SAPIENS (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.3 Å DetailsAuthors Banner, D.W. / Benz, J. / Stihle, M. CitationJournal : Bioorg.Med.Chem.Lett. / Year : 2013Title : Bace1 Inhibitors: A Head Group Scan on a Series of Amides.Authors: Woltering, T.J. / Wostl, W. / Hilpert, H. / Rogers-Evans, M. / Pinard, E. / Mayweg, A. / Gobel, M. / Banner, D.W. / Benz, J. / Travagli, M. / Pollastrini, M. / Marconi, G. / Gabellieri, E. / ... Authors : Woltering, T.J. / Wostl, W. / Hilpert, H. / Rogers-Evans, M. / Pinard, E. / Mayweg, A. / Gobel, M. / Banner, D.W. / Benz, J. / Travagli, M. / Pollastrini, M. / Marconi, G. / Gabellieri, E. / Guba, W. / Mauser, H. / Andreini, M. / Jacobsen, H. / Power, E. / Narquizian, R. History Deposition Mar 18, 2013 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jun 19, 2013 Provider : repository / Type : Initial releaseRevision 1.1 Jul 10, 2013 Group : Database referencesRevision 1.2 Jan 30, 2019 Group : Data collection / Experimental preparation / Category : exptl_crystal_grow / Item : _exptl_crystal_grow.methodRevision 1.3 Feb 6, 2019 Group : Data collection / Experimental preparation / Category : exptl_crystal_grow / Item : _exptl_crystal_grow.tempRevision 1.4 Dec 20, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description / Structure summary Category : chem_comp / chem_comp_atom ... chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_database_status / pdbx_entity_nonpoly / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site Item : _chem_comp.name / _database_2.pdbx_DOI ... _chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id Revision 1.5 Nov 20, 2024 Group : Structure summary / Category : pdbx_entry_details / pdbx_modification_feature
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.