7B4QA

Structure of a cold active hsl family esterase reveals mechanisms of low temperature adaptation and substrate specificity
Total Genus 107
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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
107
sequence length
314
structure length
314
Chain Sequence
MKNRIDPELRAMLDMFPPLNLDDVQATRKAMEEAAQLTELPVDEEVVVSNRMVPGPEDNPYVRVRIYEPKEKIEKLPGLLWIHGGGYVLGAPEGDDLLCQRFVKEANCVVVSVDYRLAPEHPYPAPLEDCYAALQWFAKKVDELGVDASRIGVGGQSAGGGLTAALALLARDRKGPELCFQMPLYPMIDDKNNSPSSLEITGNLIWNHDLNEKGWSMYLDGKNGTDDVPVHAAPARATDLTNLPYTYTCVGQLDPFRDETLDYVKRLCQAGVDVEFHLYPGAYHGFETLNPAAAVSQRALAEYVGAVKHVLNRE
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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 Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism.
pubmed doi rcsb
molecule tags Hydrolase
source organism Bacillus cohnii nbrc 15565
molecule keywords Lipase
total genus 107
structure length 314
sequence length 314
chains with identical sequence B
ec nomenclature ec 3.1.1.3: triacylglycerol lipase.
pdb deposition date 2020-12-02
Image from the rcsb pdb (www.rcsb.org)
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