Structural Classification of Proteins
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Protein: Transglutaminase catalytic domain from Human (Homo sapiens), TGase E3 [TaxId: 9606]

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Cysteine proteinases [54000]
    consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn
  4. Superfamily: Cysteine proteinases [54001]
    the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta-sheet
    link to SUPERFAMILY database - Superfamily
  5. Family: Transglutaminase core [54044]
  6. Protein: Transglutaminase catalytic domain [54045]
  7. Species: Human (Homo sapiens), TGase E3 [TaxId: 9606] [75334]

PDB Entry Domains:

  1. 1vjj picpicxrefxref
    complexed with ca, cl, gdp, mg; mutant
    1. region a:141-461 [100817] picpiclink
    2. region b:141-459 [100821] picpiclink
  2. 1sgx picpicxrefxref
    complexed with 5gp, ca, mg; mutant
    1. region a:141-461 [98865] picpiclink
    2. region b:141-459 [98869] picpiclink
  3. 1l9n picpicxrefxref
    complexed with bgl, ca, cl; mutant
    1. region a:141-460 [73743] picpiclink
    2. region b:141-460 [73747] picpiclink
  4. 1rle picpicxrefxref
    complexed with ca, gsp, mg; mutant
    1. region a:141-461 [97641] picpiclink
    2. region b:141-459 [97645] picpiclink
  5. 1l9m picpicxrefxref
    complexed with br, ca, cl; mutant
    1. region a:141-461 [73735] picpiclink
    2. region b:141-460 [73739] picpiclink
  6. 1nug picpicxrefxref
    complexed with ca, cl, mg; mutant
    1. region a:141-461 [86189] picpiclink
    2. region b:141-459 [86193] picpiclink
  7. 1nuf picpicxrefxref
    complexed with br, ca, cl; mutant
    1. region a:141-461 [86185] picpiclink
  8. 1nud picpicxrefxref
    complexed with br, ca, cl; mutant
    1. region a:141-460 [86177] picpiclink
    2. region b:141-460 [86181] 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