Structural Classification of Proteins
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Protein: Calcyclin (S100) from Human (Homo sapiens), s100a9 (mrp14) [TaxId: 9606]

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: S100 proteins [47478]
    dimer: subunits are made of two EF-hands
  6. Protein: Calcyclin (S100) [47479]
  7. Species: Human (Homo sapiens), s100a9 (mrp14) [TaxId: 9606] [69020]

PDB Entry Domains:

  1. 1xk4 picpicxrefxrefxrefxrefxrefxref
    automatically matched to d1irja_
    complexed with ca, cl, flc; mutant
    1. region c:4-86 [122057] picpiclink
  2. 1xk4 picpicxrefxrefxrefxrefxrefxref
    automatically matched to d1irja_
    complexed with ca, cl, flc; mutant
    1. region d:4-86 [122058] picpiclink
  3. 1xk4 picpicxrefxrefxrefxrefxrefxref
    automatically matched to d1irja_
    complexed with ca, cl, flc; mutant
    1. region g:4-86 [122061] picpiclink
  4. 1xk4 picpicxrefxrefxrefxrefxrefxref
    automatically matched to d1irja_
    complexed with ca, cl, flc; mutant
    1. region h:4-86 [122062] picpiclink
  5. 1xk4 picpicxrefxrefxrefxrefxrefxref
    automatically matched to d1irja_
    complexed with ca, cl, flc; mutant
    1. region k:4-86 [122065] picpiclink
  6. 1xk4 picpicxrefxrefxrefxrefxrefxref
    automatically matched to d1irja_
    complexed with ca, cl, flc; mutant
    1. region l:4-86 [122066] picpiclink
  7. 1irj picpic
    complexed with ca, cps
    1. chain a [66289] picpiclink
    2. chain b [66290] picpiclink
    3. chain c [66291] picpiclink
    4. chain d [66292] picpiclink
    5. chain e [66293] picpiclink
    6. chain f [66294] picpiclink
    7. chain g [66295] picpiclink
    8. chain h [66296] 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