Structural Classification of Proteins
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Protein: Calmodulin from African frog (Xenopus laevis) [TaxId: 8355]

Lineage:

  1. Root: scop
  2. Class: All alpha proteins [46456]
  3. Fold: EF Hand-like [47472]
    core: 4 helices; array of 2 hairpins, opened
  4. Superfamily: EF-hand [47473]
    Duplication: consists of two EF-hand units: each is made of two helices connected with calcium-binding loop
    link to SUPERFAMILY database - Superfamily
  5. Family: Calmodulin-like [47502]
    Duplication: made with two pairs of EF-hands
  6. Protein: Calmodulin [47516]
  7. Species: African frog (Xenopus laevis) [TaxId: 8355] [47521]

PDB Entry Domains:

  1. 1iq5 picpic
    complex with a ca2+/calmodulin dependent kinase kinase fragment
    complexed with ca
    1. chain a [62643] picpiclink
  2. 2ggm picpic
    automatically matched to d1cfc__
    complexed with ca
    1. region a:24-166 [135152] picpiclink
  3. 2ggm picpic
    automatically matched to d1cfc__
    complexed with ca
    1. region b:25-166 [135153] picpiclink
  4. 1f70 picpic
    N-terminal domain
    1. chain a [17288] picpiclink
  5. 1f71 picpic
    C-terminal domain
    1. chain a [17289] picpiclink
  6. 1nwd picpic
    complex with the C-terminal fragment of glutamate decarboxylase, chains B and C
    complexed with ca
    1. chain a [86297] picpiclink
  7. 2k3s picpic
    automatically matched to d1cmfa_
    1. region b:82-148 [148267] picpiclink
  8. 1cfc picpic
    1. chain a [17290] picpiclink
  9. 1mux picpic
    complexed with ca, ww7
    1. chain a [17292] picpiclink
  10. 1cfd picpic
    1. chain a [17291] picpiclink
  11. 1dmo picpic
    1. chain a [17293] picpiclink
  12. 1ckk picpic
    complex with a fragment of the rat ca2+/calmodulin dependent protein kinase
    complexed with ca
    1. chain a [17294] picpiclink
  13. 1cff picpic
    complex with a binding peptide of the human Ca2+-pump
    complexed with ca
    1. chain a [17295] 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