Structural Classification of Proteins
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Family: Pseudouridine synthase I TruA

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Pseudouridine synthase [100877]
    consists of two alpha+beta subdomains with some similarity to the ferredoxin-like fold
  4. Superfamily: Pseudouridine synthase [55120]
    the active site is the most conserved structural region of the superfamily and is located between the subdomains
    link to SUPERFAMILY database - Superfamily
  5. Family: Pseudouridine synthase I TruA [55121]

Protein Domains:

  1. Pseudouridine synthase I TruA [55122]
    1. Escherichia coli [TaxId: 562] [55123] (10)
      1. 1dj0 picpic
        complexed with cl
        1. chain a [90337] picpiclink
        2. chain b [90338] picpiclink
      2. 2nqp picpic
        automatically matched to d1dj0a_
        complexed with k
        1. region a:7-270 [138474] picpiclink
      3. 2nqp picpic
        automatically matched to d1dj0a_
        complexed with k
        1. region b:7-270 [138475] picpiclink
      4. 2nqp picpic
        automatically matched to d1dj0a_
        complexed with k
        1. region c:7-270 [138476] picpiclink
      5. 2nqp picpic
        automatically matched to d1dj0a_
        complexed with k
        1. region d:8-270 [138477] picpiclink
      6. 2nr0 picpic
        automatically matched to d1dj0a_
        1. region a:7-270 [138514] picpiclink
      7. 2nr0 picpic
        automatically matched to d1dj0a_
        1. region b:7-270 [138515] picpiclink
      8. 2nr0 picpic
        automatically matched to d1dj0a_
        1. region c:7-270 [138516] picpiclink
      9. 2nr0 picpic
        automatically matched to d1dj0a_
        1. region d:7-270 [138517] picpiclink
      10. 2nre picpic
        automatically matched to d1dj0a_
        complexed with k
        1. region a:7-270 [138520] 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