Structural Classification of Proteins
Fold: Antiparallel coiled-coil
this is not a true fold; contains at least two very long antiparallel helices
Lineage:
Root:
scop
Class:
Coiled coil proteins
[57942]
Not a true class
Fold:
Antiparallel coiled-coil
[58086]
this is not a true fold; contains at least two very long antiparallel helices
Superfamilies:
Variant surface glycoprotein (N-terminal domain)
[58087] (1)
Clostridium neurotoxins, "coiled-coil" domain
[58091] (1)
Colicin Ia, N-terminal domain
[58096] (1)
Colicin E3 receptor domain
[69985] (1)
Hemolysin E (HlyE, ClyA, SheA)
[58100] (1)
Methyl-accepting chemotaxis protein (MCP) signaling domain
[58104] (1)
Oligomerization domain of hepatitis delta antigen
[58108] (1)
F1 ATPase inhibitor, IF1, C-terminal domain
[64602] (1)
Chemotaxis phosphatase CheZ
[75708] (1)
dimerizes with the formation of a 4-helical bundle
Rad50 coiled-coil Zn hook
[75712] (1)
dimerizes via a CxxC motif in the loop, zinc-hook
C-terminal domain of PLC-beta
[69989] (1)
left-handed antiparallel coiled-coil; dimerizes with the formation of a 4-helical bundle
Tumor suppressor gene product Apc
[82931] (1)
Proline/betaine transporter ProP, C-terminal cytoplasmic domain
[103661] (1)
Fzo-like conserved region
[111479] (1)
antiparallel coiled-coil in the crystals
occludin/ELL-like
[144292] (1)
antiparallel hairpin with a kinked second helix; similar to the N-terminal structure of the thermostable carboxypeptidase 1 (scop_pr 82731)
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Generated from scop database 1.73 with scopm 1.101 on Wed Nov 21 11:18:32 2007
Copyright
© 1994-2007 The scop authors / scop@mrc-lmb.cam.ac.uk