6KJBA

Wild-type apo-form e. coli atcase holoenzyme with an unusual open conformation of r167
Total Genus 106
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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
106
sequence length
309
structure length
300
Chain Sequence
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLV
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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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molecule tags Transferase
molecule keywords Aspartate carbamoyltransferase catalytic subunit
publication title Conformational Plasticity of the Active Site Entrance inE. coliAspartate Transcarbamoylase and Its Implication in Feedback Regulation.
pubmed doi rcsb
source organism Escherichia coli k-12
total genus 106
structure length 300
sequence length 309
ec nomenclature ec 2.1.3.2: Aspartate carbamoyltransferase.
pdb deposition date 2019-07-22

pfam database annotations

chain Pfam Accession Code Pfam Family Identifier Pfam Description
A PF00185 OTCace Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain
A PF02729 OTCace_N Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain
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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