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==About this Structure== | ==About this Structure== | ||
[[2zta]] is composed of two identical 52 residue alpha helix chains that grouped together to form a dimer. The dimer binds through interlocking leucine amino acids in the C terminal ends, while pinching in on the major groove of DNA in the N terminal end. | |||
GCN4 (PDB [[2zta]] by itself, [[1ysa]] bound to DNA) is a eukaryotic transcription factor first isolated from yeast. It is composed of two identical 52 residue alpha helix chains that grouped together to form a dimer. The dimer binds through interlocking leucine amino acids in the C terminal ends, while pinching in on the major groove of DNA in the N terminal end. | |||
Revision as of 03:43, 9 November 2011
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2zta, resolution 1.80Å () | |||||||
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Non-Standard Residues: | |||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||
Coordinates: | save as pdb, mmCIF, xml |
GCN4 - Leucine ZipperGCN4 - Leucine Zipper
Blah blah information about leucine zipper GCN4.
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1ysa, resolution 2.90Å () | |||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
About this StructureAbout this Structure
GCN4 (PDB 2zta by itself, 1ysa bound to DNA) is a eukaryotic transcription factor first isolated from yeast. It is composed of two identical 52 residue alpha helix chains that grouped together to form a dimer. The dimer binds through interlocking leucine amino acids in the C terminal ends, while pinching in on the major groove of DNA in the N terminal end.