Structural Classification of Proteins
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Protein: Feruloyl esterase domain of the cellulosomal xylanase y from Clostridium thermocellum [TaxId: 1515]

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: alpha/beta-Hydrolases [53473]
    core: 3 layers, a/b/a; mixed beta-sheet of 8 strands, order 12435678, strand 2 is antiparallel to the rest
  4. Superfamily: alpha/beta-Hydrolases [53474]
    many members have left-handed crossover connection between strand 8 and additional strand 9
    link to SUPERFAMILY database - Superfamily
  5. Family: Carboxylesterase [53487]
  6. Protein: Feruloyl esterase domain of the cellulosomal xylanase y [69579]
  7. Species: Clostridium thermocellum [TaxId: 1515] [69580]

PDB Entry Domains:

  1. 1wb4 picpic
    automatically matched to d1gkla_
    complexed with acy, cd, gol, sxx; mutant
    1. region a:803-1075 [120827] picpiclink
  2. 1wb4 picpic
    automatically matched to d1gkla_
    complexed with acy, cd, gol, sxx; mutant
    1. region b:803-1075 [120828] picpiclink
  3. 1wb6 picpic
    automatically matched to d1gkla_
    complexed with act, cd, gol, vxx; mutant
    1. region a:803-1075 [120831] picpiclink
  4. 1wb6 picpic
    automatically matched to d1gkla_
    complexed with act, cd, gol, vxx; mutant
    1. region b:803-1075 [120832] picpiclink
  5. 1wb5 picpic
    automatically matched to d1gkla_
    complexed with act, cd, gol, syr; mutant
    1. region a:803-1075 [120829] picpiclink
  6. 1wb5 picpic
    automatically matched to d1gkla_
    complexed with act, cd, gol, syr; mutant
    1. region b:803-1075 [120830] picpiclink
  7. 1gkl picpic
    complexed with acy, cd, fer, gol; mutant
    1. chain a [65250] picpiclink
    2. chain b [65251] picpiclink
  8. 1gkk picpic
    complexed with cd, gol
    1. chain a [65248] picpiclink
    2. chain b [65249] 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