Entry | Database: PDB / ID: 4inr |
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Title | Yeast 20S proteasome in complex with the vinyl sulfone LU102 |
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Components | (Proteasome component ... ) x 14 |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / UPS / drug discovery / irreversible inhibition / Ntn hydrolase / non-lysosomal protein breakdown / HYDROLASE-HYDROLASE INHIBITOR complex |
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Function / homology | Function and homology information
proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / Ub-specific processing proteases ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / Ub-specific processing proteases / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / proteasomal protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol / cytoplasmSimilarity search - Function Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. ... Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha BetaSimilarity search - Domain/homologyN3PHE-LEU-LEU-PHE(4-NH2CH2)-METHYL VINYL SULFONE, BOUND FORM / Chem-1G1 / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 ...N3PHE-LEU-LEU-PHE(4-NH2CH2)-METHYL VINYL SULFONE, BOUND FORM / Chem-1G1 / Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 / Proteasome subunit beta type-7 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4Similarity search - Component |
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Biological species | ![](img/tx_yeast.gif) ![](data/taxo/icon/Saccharomyces_cerevisiae_S.png) Saccharomyces cerevisiae (brewer's yeast) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å |
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Authors | Geurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E.M. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. ...Geurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E.M. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. / Driessen, C. / van der Stelt, M. / Groll, M. / Overkleeft, H.S. / Kisselev, A.F. |
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Citation | Journal: J.Med.Chem. / Year: 2013 Title: Incorporation of Non-natural Amino Acids Improves Cell Permeability and Potency of Specific Inhibitors of Proteasome Trypsin-like Sites. Authors: Geurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. / Driessen, C. / van der ...Authors: Geurink, P.P. / van der Linden, W.A. / Mirabella, A.C. / Gallastegui, N. / de Bruin, G. / Blom, A.E. / Voges, M.J. / Mock, E.D. / Florea, B.I. / van der Marel, G.A. / Driessen, C. / van der Stelt, M. / Groll, M. / Overkleeft, H.S. / Kisselev, A.F. |
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History | Deposition | Jan 6, 2013 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jan 30, 2013 | Provider: repository / Type: Initial release |
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Revision 1.1 | Feb 27, 2013 | Group: Database references |
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Revision 1.2 | Sep 20, 2023 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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