7AOUA

The fk1 domain of fkbp51 in complex with (2'r,5's,12'r)-12'-cyclohexyl-2'-[2-(3,4-dimethoxyphenyl)ethyl]-3',19'-dioxa-10',13',16'-triazaspiro[cyclopropane-1,15'- tricyclo[18.3.1.0-5,10]tetracosane]-1'(24'),20',22'-triene-4',11',14',17'-tetrone
Total Genus 29
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The genus trace: a function that shows values of genus (vertical axis) for subchains spanned between the first residue, and all other residues (shown on horizontal axis). The number of the latter residue and the genus of a given subchain are shown interactively.

Total Genus
29
sequence length
128
structure length
128
Chain Sequence
GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGE
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The genus matrix. At position (x,y) a genus value for a subchain spanned between x’th and y’th residue is shown. Values of the genus are represented by color, according to the scale given on the right.

Structure visualization

After clicking on a point (x,y) in the genus matrix above, a subchain from x to y is shown in color.

Chord Diagram
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publication title Macrocyclic FKBP51 ligands define a transient binding mode with enhanced selectivity.
pubmed doi rcsb
molecule tags Isomerase
source organism Homo sapiens
molecule keywords Peptidyl-prolyl cis-trans isomerase FKBP5
total genus 29
structure length 128
sequence length 128
ec nomenclature ec 5.2.1.8: Peptidylprolyl isomerase.
pdb deposition date 2020-10-15
Image from the rcsb pdb (www.rcsb.org)
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similar chains in the Genus database (?% sequence similarity)
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similar chains in the pdb database (?% sequence similarity)

 
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#similar chains, but unknotted
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