5VMQA

Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution
Total Genus 103
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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
103
sequence length
310
structure length
298
Chain Sequence
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSAGETLADTISVISTYVDAIVMAHPQEGAARLATEFSGNVPVLNAGHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL
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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
publication title Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
pubmed doi rcsb
source organism Escherichia coli o45:k1 (strain s88 / expec)
total genus 103
structure length 298
sequence length 310
chains with identical sequence B, C
ec nomenclature ec 2.1.3.2: Aspartate carbamoyltransferase.
pdb deposition date 2017-04-28

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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