Structural Classification of Proteins




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:
- Root: scop
- Class: Alpha and beta proteins (a/b)
Mainly parallel beta sheets (beta-alpha-beta units)
- 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:
- Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) (1)
domain 2 contains the P-loop ATP-binding motif
- Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) (1)
- Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase)
- Escherichia coli (3)
- 1ayl



complexed with atp, mg, oxl
- 1oen



complexed with act
- 1aq2



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