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Bryan Toton (talk | contribs) Tertiary structure of PAL. The three central core helices, leading to the active site, are colored blue, green, and yellow for emphasis. (a) Stereoview of the PAL monomer with residue numbering. Breaks in the polypeptide chain are indicated by asterisks. |
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== Licensing == | == Licensing == | ||
{{subst:Non-commercial from license selector}} | {{subst:Non-commercial from license selector}} | ||
Calabrese et al <ref name=crystal>http://pubs.acs.org.prox.lib.ncsu.edu/doi/pdfplus/10.1021/bi049053%2B</ref> |
Latest revision as of 16:39, 6 December 2013
SummarySummary
Tertiary structure of PAL. The three central core helices, leading to the active site, are colored blue, green, and yellow for emphasis. (a) Stereoview of the PAL monomer with residue numbering. Breaks in the polypeptide chain are indicated by asterisks. (b) Close-up stereoview of MIO and Phe413 interactions with the three central helices, polarized with their N termini directed toward the active site. Hydrogen bonds are indicated by dashed lines.
LicensingLicensing
{{subst:Non-commercial from license selector}}
Calabrese et al [1]
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current | 16:37, 6 December 2013 | ![]() | 500 × 654 (78 KB) | Bryan Toton (talk | contribs) | Tertiary structure of PAL. The three central core helices, leading to the active site, are colored blue, green, and yellow for emphasis. (a) Stereoview of the PAL monomer with residue numbering. Breaks in the polypeptide chain are indicated by asterisks. |
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