Structural Classification of Proteins
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Protein: 5'-nucleotidase (syn. UDP-sugar hydrolase), N-terminal domain from Escherichia coli [TaxId: 562]

SQ P07024 26-550

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Metallo-dependent phosphatases [56299]
    4 layers: alpha/beta/beta/alpha; mixed beta sheets; contains duplication
  4. Superfamily: Metallo-dependent phosphatases [56300]
    different families of this superfamily are groupped in a single Pfam family, Pfam 00149
    link to SUPERFAMILY database - Superfamily
  5. Family: 5'-nucleotidase (syn. UDP-sugar hydrolase), N-terminal domain [56307]
  6. Protein: 5'-nucleotidase (syn. UDP-sugar hydrolase), N-terminal domain [56308]
  7. Species: Escherichia coli [TaxId: 562] [56309]
    SQ P07024 26-550

PDB Entry Domains:

  1. 1ush picpicxref
    complexed with co3, so4, zn
    1. region a:26-362 [42079] picpiclink
  2. 1hp1 picpicxref
    complexed with atp, co3, so4, zn
    1. region a:26-362 [70977] picpiclink
  3. 1hpu picpicxref
    complexed with a12, mn
    1. region a:26-362 [70980] picpiclink
    2. region b:26-362 [70982] picpiclink
    3. region c:26-362 [70984] picpiclink
    4. region d:26-362 [70986] picpiclink
  4. 1oi8 picpicxref
    complexed with co3, mn, so4; mutant
    1. region a:26-362 [103943] picpiclink
    2. region b:26-362 [103945] picpiclink
  5. 2ush picpicxref
    complexed with wo4, zn
    1. region a:26-362 [42080] picpiclink
    2. region b:26-362 [42081] picpiclink
  6. 1oid picpicxref
    complexed with ni; mutant
    1. region a:26-362 [103953] picpiclink
    2. region b:26-362 [103955] picpiclink
  7. 1oie picpicxref
    complexed with ni; mutant
    1. region a:26-362 [103957] picpiclink
  8. 1ho5 picpicxref
    complexed with adn, mn, po4
    1. region a:26-362 [70969] picpiclink
    2. region b:26-362 [70971] 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