Structural Classification of Proteins
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Protein: Butyryl cholinesterase from Human (Homo sapiens) [TaxId: 9606]

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: Acetylcholinesterase-like [53475]
  6. Protein: Butyryl cholinesterase [102612]
  7. Species: Human (Homo sapiens) [TaxId: 9606] [102613]

PDB Entry Domains:

  1. 1p0i picpic
    complexed with bua, cl, fuc, gol, mes, nag, sul; mutant
    1. chain a [93867] picpiclink
  2. 1xlw picpic
    automatically matched to d1p0ia_
    complexed with cl, dep, fuc, ful, gol, nag, s, so4; mutant
    1. region a:4-529 [122139] picpiclink
  3. 1xlu picpic
    automatically matched to d1p0ia_
    complexed with cl, ful, gol, mip, nag, s, so4; mutant
    1. region a:4-529 [122137] picpiclink
  4. 1xlv picpic
    automatically matched to d1p0ia_
    complexed with cl, efs, ful, gol, nag, s, so4; mutant
    1. region a:4-529 [122138] picpiclink
  5. 1p0p picpic
    complexed with bch, cl, fuc, gol, nag, som, sul; mutant
    1. chain a [93869] picpiclink
  6. 1p0q picpic
    complexed with cl, fuc, gol, nag, som, sul; mutant
    1. chain a [93870] picpiclink
  7. 1p0m picpic
    complexed with cht, cl, fuc, gol, mes, nag, sul; mutant
    1. chain a [93868] picpiclink
  8. 2pm8 picpic
    automatically matched to d1p0ia_
    complexed with gol, nag, ndg, so4
    1. region a:4-529 [149655] picpiclink
  9. 2pm8 picpic
    automatically matched to d1p0ia_
    complexed with gol, nag, ndg, so4
    1. region b:4-529 [149656] 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