Structural Classification of Proteins
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Fold: OB-fold

barrel, closed or partly opened n=5, S=10 or S=8; greek-key

Lineage:

  1. Root: scop
  2. Class: All beta proteins [48724]
  3. Fold: OB-fold [50198]
    barrel, closed or partly opened n=5, S=10 or S=8; greek-key

Superfamilies:

  1. Staphylococcal nuclease [50199] (1) picpic
    link to SUPERFAMILY database - Superfamily
  2. Bacterial enterotoxins [50203] (2) picpic
    link to SUPERFAMILY database - Superfamily
  3. TIMP-like [50242] (3) picpic
    link to SUPERFAMILY database - Superfamily
  4. Heme chaperone CcmE [82093] (1) picpic
    link to SUPERFAMILY database - Superfamily
  5. gp5 N-terminal domain-like [69255] (1) picpic
    link to SUPERFAMILY database - Superfamily
  6. Hypothetical protein YgiW [101756] (1) picpic
    link to SUPERFAMILY database - Superfamily
  7. Nucleic acid-binding proteins [50249] (16) picpic
    link to SUPERFAMILY database - Superfamily
  8. Inorganic pyrophosphatase [50324] (1) picpic
    link to SUPERFAMILY database - Superfamily
  9. MOP-like [50331] (3) picpic
    link to SUPERFAMILY database - Superfamily
  10. CheW-like [50341] (1) picpic
    link to SUPERFAMILY database - Superfamily
  11. TM0957-like [141318] (1) picpic
    extra N-terminal region and large insertion after strand 3 together form an alpha-helical subdomain
    link to SUPERFAMILY database - Superfamily
  12. NfeD domain-like [141322] (1) picpic
    close structural similarity to some members of the Nucleic acid-binding OB-fold proteins, possibly related to this superfamily
    link to SUPERFAMILY database - Superfamily
  13. BC4932-like [159121] (1) picpic
  14. HupF/HypC-like [159127] (1) picpic
    contains extra C-terminal helix packed against the beta-barrel side
  15. EutN/CcmL-like [159133] (1) picpic
    homohexameric unit
  16. HIN-2000 domain-like [159141] (1) picpic
    duplication: tandem repeat of two OB-fold domains

Enter search key:

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