5M99A

Functional characterization and crystal structure of thermostable amylase from thermotoga petrophila, reveals high thermostability and an archaic form of dimerization
Total Genus 195
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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
195
sequence length
506
structure length
506
Chain Sequence
NEVKYPVVYEIFIRSLYDSDGDGVGDINGVSQKVDYLRKLGIDAVWFMPFNEAVSYHGYDITDYYNVEKDYGTMEDLENMIQVLHENGIKVIMDLVINHTSDEHPWFKDAVENTTSSPYWDYYIMSLEDHSGQDHWHWKINSKGQKVWYFGLFGYNMPDLNHDSQKVREEVKKIVDFWISKGVDGFRIDAAKHIYGWSWDDGIQESAEYFEWFRDYVLSKKPDAILVGEVFSGNTYDLSLYPIPVFNFALMYSIRNYPEGQDGMIENNWVEESFLFLENHDLHRFFSHLQEHYKKFSESDYEFIKKRAALWYFLIFTLKGSPVIYYGGEIGTRGFKWHGPVYDEPVREPMQWYASGTGEGQTFWTKEVYKNAGITFGNADVDGCIYDDPYDGFSVEEQENDPKSLLNFIRFILNFRKDHDAILNGDQTIFRDWKNLIAFYRESSNEKLLVVLNPDPVWQNSFTFEENMTMILEVDFENFIWNESNVSFSAGESFTVDPMKAYIFKK
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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.

molecule tags Hydrolase
molecule keywords Alpha-amylase
publication title Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization.
pubmed doi rcsb
source organism Thermotoga petrophila rku-1
total genus 195
structure length 506
sequence length 506
ec nomenclature ec 3.2.1.1: Alpha-amylase.
pdb deposition date 2016-11-01

pfam database annotations

chain Pfam Accession Code Pfam Family Identifier Pfam Description
A PF00128 Alpha-amylase Alpha amylase, catalytic domain
Image from the rcsb pdb (www.rcsb.org)
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