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Chain R, Proteasome subunit alpha type-5

PDB: 4QW4_R

Identical Proteins FASTA Graphics 

LOCUS       4QW4_R                   260 aa            linear   PLN 20-SEP-2023
DEFINITION  Chain R, Proteasome subunit alpha type-5.
ACCESSION   4QW4_R
VERSION     4QW4_R
DBSOURCE    pdb: molecule 4QW4, chain R, release Sep 20, 2023;
            deposition: Jul 16, 2014;
            class: HYDROLASE/HYDROLASE INHIBITOR;
            source: Mmdb_id: 126674, Pdb_id 1: 4QW4;
            Exp. method: X-ray Diffraction.
KEYWORDS    .
SOURCE      Saccharomyces cerevisiae S288C
  ORGANISM  Saccharomyces cerevisiae S288C
            Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
            Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
            Saccharomyces.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Huber,E.M., Heinemeyer,W. and Groll,M.
  TITLE     Bortezomib-resistant mutant proteasomes: structural and biochemical
            evaluation with carfilzomib and ONX 0914
  JOURNAL   Structure 23 (2), 407-417 (2015)
   PUBMED   25599643
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Huber,E.M., Heinemeyer,W. and Groll,M.
  TITLE     Direct Submission
  JOURNAL   Submitted (16-JUL-2014)
COMMENT     yCP in complex with carfilzomib.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Saccharomyces cerevisiae S288C"
                     /db_xref="taxon:559292"
     Region          8..222
                     /region_name="proteasome_alpha_type_5"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03753"
                     /db_xref="CDD:239722"
     Site            order(10..13,15..16,18..19,23,26,29..30,33,41,56,58..59,
                     82..84,86..87,118,121,124..125,134..138,156,161..162,164,
                     166..167,169)
                     /site_type="other"
                     /note="alpha subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239722"
     SecStr          14..17
                     /sec_str_type="sheet"
                     /note="strand 189"
     SecStr          19..22
                     /sec_str_type="sheet"
                     /note="strand 190"
     SecStr          23..33
                     /sec_str_type="helix"
                     /note="helix 88"
     Site            order(35,51,53,66,174)
                     /site_type="active"
                     /db_xref="CDD:239722"
     SecStr          35..43
                     /sec_str_type="sheet"
                     /note="strand 191"
     SecStr          44..52
                     /sec_str_type="sheet"
                     /note="strand 192"
     SecStr          66..71
                     /sec_str_type="sheet"
                     /note="strand 193"
     SecStr          73..81
                     /sec_str_type="sheet"
                     /note="strand 194"
     SecStr          86..102
                     /sec_str_type="helix"
                     /note="helix 89"
     SecStr          109..117
                     /sec_str_type="helix"
                     /note="helix 90"
     SecStr          139..148
                     /sec_str_type="sheet"
                     /note="strand 195"
     SecStr          152..160
                     /sec_str_type="sheet"
                     /note="strand 196"
     SecStr          162..167
                     /sec_str_type="sheet"
                     /note="strand 197"
     SecStr          168..174
                     /sec_str_type="sheet"
                     /note="strand 198"
     SecStr          176..186
                     /sec_str_type="helix"
                     /note="helix 91"
     SecStr          193..207
                     /sec_str_type="helix"
                     /note="helix 92"
     SecStr          216..224
                     /sec_str_type="sheet"
                     /note="strand 199"
     SecStr          225..231
                     /sec_str_type="sheet"
                     /note="strand 200"
     SecStr          233..248
                     /sec_str_type="helix"
                     /note="helix 93"
ORIGIN      
        1 mfltrseydr gvstfspegr lfqveyslea iklgstaigi atkegvvlgv ekratsplle
       61 sdsiekivei drhigcamsg ltadarsmie hartaavthn lyydedinve sltqsvcdla
      121 lrfgegasge erlmsrpfgv alliaghdad dgyqlfhaep sgtfyrynak aigsgsegaq
      181 aellnewhss ltlkeaellv lkilkqvmee kldennaqls citkqdgfki ydnektaeli
      241 kelkekeaae speeadvems
//
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