Structural Classification of Proteins
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Superfamily: Oxysterol-binding protein-like

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: Oxysterol-binding protein-like [143999]
    core: large meander beta-sheet of 12 strands wrapped around the N-terminal (distorted) alpha-hairpin; some similarity to transmembrane beta-barrel proteins
  4. Superfamily: Oxysterol-binding protein-like [144000]
    link to SUPERFAMILY database - Superfamily

Families:

  1. Oxysterol-binding protein [144001] (1)
    Pfam 01237
    1. Oxysterol-binding protein homolog 4, KES1 [144002]
      1. Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932] [144003] (8)
        SQ P35844 2-434! SQ P35844 30-434
        1. 1zhx picpic
          automatically matched to 1ZHT A:2-434
          complexed with hc3
          1. region a:2-434 [125112] picpiclink
        2. 1zhy picpic
          automatically matched to 1ZHT A:2-434
          complexed with clr, pb
          1. region a:2-434 [125113] picpiclink
        3. 1zhw picpic
          automatically matched to 1ZHT A:2-434
          complexed with hc2, pb
          1. region a:2-434 [125111] picpiclink
        4. 1zhz picpic
          automatically matched to 1ZHT A:2-434
          complexed with erg, pb
          1. region a:2-434 [125114] picpiclink
        5. 1zht picpic
          complexed with hcr
          1. region a:2-434 [125108] picpiclink
        6. 1zi7 picpic
          complexed with so4; mutant
          1. region a:30-434 [125119] picpiclink
        7. 1zi7 picpic
          automatically matched to 1ZI7 A:30-434
          complexed with so4; mutant
          1. region b:34-434 [125120] picpiclink
        8. 1zi7 picpic
          automatically matched to 1ZI7 A:30-434
          complexed with so4; mutant
          1. region c:34-434 [125121] picpiclink

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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