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Publication Abstract from PubMed
The three dimensional structure of the N-terminal domain (residues 1-42) of the copper-responsive transcription factor Amtl from Candida glabrata has been determined by two-dimensional 1H-correlated nuclear magnetic resonance (NMR) methods. The domain contains an array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) that is conserved among a family of Cu-responsive transcription factors. The structure is unlike those of previously characterized zinc finger motifs, and consists of a three-stranded antiparallel beta-sheet with two short helical segments that project from one end of the beta-sheet. Conserved residues at positions 16, 18 and 19 form a basic patch that may be important for DNA binding.
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors.,Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:9665167[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR. Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors. Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:9665167 doi:10.1038/805
