Structural Classification of Proteins
Fold: Non-globular all-alpha subunits of globular proteins
not a true fold
Lineage:
Root:
scop
Class:
All alpha proteins
[46456]
Fold:
Non-globular all-alpha subunits of globular proteins
[48661]
not a true fold
Superfamilies:
Ribosomal protein L39e
[48662] (1)
interrupted alpha-helix
uperfamily
Ribosomal protein L39e
[48663] (1)
Methanol dehydrogenase subunit
[48666] (1)
consists of single alpha-helix and irregular N-terminal tail
uperfamily
Methanol dehydrogenase subunit
[48667] (3)
Transducin (heterotrimeric G protein), gamma chain
[48670] (1)
long alpha-helix interrupted in the middle
uperfamily
Transducin (heterotrimeric G protein), gamma chain
[48671] (2)
Fe-only hydrogenase smaller subunit
[48674] (1)
uperfamily
Fe-only hydrogenase smaller subunit
[48675] (1)
Moesin tail domain
[48678] (1)
uperfamily
Moesin tail domain
[48679] (1)
Proteinase A inhibitor IA3
[48686] (1)
uperfamily
Proteinase A inhibitor IA3
[48687] (1)
Epsilon subunit of mitochondrial F1F0-ATP synthase
[48690] (1)
uperfamily
Epsilon subunit of mitochondrial F1F0-ATP synthase
[48691] (1)
Quinohemoprotein amine dehydrogenase C chain
[69131] (1)
uperfamily
Quinohemoprotein amine dehydrogenase C chain
[69132] (2)
Stathmin
[101494] (1)
single long helix crosslinking four tubulin subunits
uperfamily
Stathmin
[101495] (1)
Anti-sigma factor FlgM
[101498] (1)
uperfamily
Anti-sigma factor FlgM
[101499] (1)
Glu-tRNAGln amidotransferase C subunit
[141000] (1)
uperfamily
Glu-tRNAGln amidotransferase C subunit
[141001] (1)
Pfam 02686
RelB-like
[141004] (1)
wraps around RelE subunit
uperfamily
RelB-like
[141005] (1)
Lag-3 N-terminal region
[158851] (1)
long kinked helix, part of the CSL-Notch-Mastermind ternary complex
Lag-3 N-terminal region
[158852] (1)
Lipase chaperone-like
[158855] (1)
open single layer scaffold of 11 helices, which engulfs the substrate protein
Lipase chaperone LifO-like
[158856] (1)
Pfam 03280
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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