Structural Classification of Proteins
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Protein: Histidyl-tRNA synthetase (HisRS), C-terminal domain from Escherichia coli [TaxId: 562]

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: Anticodon-binding domain-like [52953]
    3 layers: a/b/a; mixed beta-sheet of five strands, order 21345; strand 4 is antiparallel to the rest
  4. Superfamily: Class II aaRS ABD-related [52954]
    link to SUPERFAMILY database - Superfamily
  5. Family: Anticodon-binding domain of Class II aaRS [52955]
  6. Protein: Histidyl-tRNA synthetase (HisRS), C-terminal domain [52956]
  7. Species: Escherichia coli [TaxId: 562] [52957]

PDB Entry Domains:

  1. 1kmm picpicxref
    complexed with ham
    1. region a:326-424 [33174] picpiclink
    2. region b:326-424 [33175] picpiclink
    3. region c:326-424 [33176] picpiclink
    4. region d:326-424 [33177] picpiclink
  2. 2el9 picpicxrefxrefxrefxref
    automatically matched to d1htta1
    complexed with hss
    1. region a:326-424 [146887] picpiclink
  3. 2el9 picpicxrefxrefxrefxref
    automatically matched to d1htta1
    complexed with hss
    1. region b:326-424 [146889] picpiclink
  4. 2el9 picpicxrefxrefxrefxref
    automatically matched to d1htta1
    complexed with hss
    1. region c:326-424 [146891] picpiclink
  5. 2el9 picpicxrefxrefxrefxref
    automatically matched to d1htta1
    complexed with hss
    1. region d:326-424 [146893] picpiclink
  6. 1htt picpicxref
    complexed with amp
    1. region a:326-424 [33178] picpiclink
    2. region b:326-424 [33179] picpiclink
    3. region c:326-424 [33180] picpiclink
    4. region d:326-424 [33181] picpiclink
  7. 1kmn picpicxref
    complexed with atp, hso
    1. region a:326-424 [33182] picpiclink
    2. region b:326-424 [33183] picpiclink
    3. region c:326-424 [33184] picpiclink
    4. region d:326-424 [33185] 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