Structural Classification of Proteins
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Fold: Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase)

consists of two alpa/beta domains
duplication: the domains share an unusual fold of 2 helices and 6-stranded mixed sheet; beta(2)-alpha-beta(4)-alpha; order 312465, strands 1 and 5 are antiparallel to the rest

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b)
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase)
    consists of two alpa/beta domains
    duplication: the domains share an unusual fold of 2 helices and 6-stranded mixed sheet; beta(2)-alpha-beta(4)-alpha; order 312465, strands 1 and 5 are antiparallel to the rest

Superfamilies:

  1. Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) (1)
    domain 2 contains the P-loop ATP-binding motif
    1. Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) (1)
      1. Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase)
        1. Escherichia coli (3)
          1. 1ayl seq
            complexed with atp, mg, oxl
          2. 1oen seq
            complexed with act
          3. 1aq2 seq
            complexed with atp, mg, mn, pyr

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Generated from scop database 1.55 with scopm 1.095 on Mon Jul 9 18:35:50 2001
Copyright © 1994-2001 The scop authors / scop@mrc-lmb.cam.ac.uk