Structural Classification of Proteins
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Superfamily: Multidrug efflux transporter AcrB TolC docking domain; DN and DC subdomains

duplication: the N- and C-terminal halves of the whole proteins are structurally similar
link to SUPERFAMILY database - Superfamily

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Multidrug efflux transporter AcrB TolC docking domain; DN and DC subdomains [82713]
    Intertwined pseudo hexamer of an alpha+beta motif
  4. Superfamily: Multidrug efflux transporter AcrB TolC docking domain; DN and DC subdomains [82714]
    duplication: the N- and C-terminal halves of the whole proteins are structurally similar
    link to SUPERFAMILY database - Superfamily

Families:

  1. Multidrug efflux transporter AcrB TolC docking domain; DN and DC subdomains [82715] (1)
    1. Multidrug efflux transporter AcrB TolC docking domain; DN and DC subdomains [82716]
      1. Escherichia coli [TaxId: 562] [82717] (6)
        1. 1iwg picpicxrefxref
          1. region a:182-273 [76878] picpiclink
          2. region a:725-812 [76879] picpiclink
        2. 1oy8 picpicxrefxref
          complexed with rhq
          1. region a:182-273 [87567] picpiclink
          2. region a:725-812 [87568] picpiclink
        3. 1oy6 picpicxrefxref
          1. region a:182-273 [87559] picpiclink
          2. region a:725-812 [87560] picpiclink
        4. 1oye picpicxrefxref
          complexed with cpf
          1. region a:182-273 [87591] picpiclink
          2. region a:725-812 [87592] picpiclink
        5. 1oy9 picpicxrefxref
          complexed with et
          1. region a:182-273 [87575] picpiclink
          2. region a:725-812 [87576] picpiclink
        6. 1oyd picpicxrefxref
          complexed with deq
          1. region a:182-273 [87583] picpiclink
          2. region a:725-812 [87584] picpiclink

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MRC
site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk