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 |
27
|
sequence length |
153
|
structure length |
153
|
Chain Sequence |
b'MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEPVSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN'
|
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.
After clicking on a point (x,y) in the genus matrix above, a subchain from x to y is shown in color.
| publication title |
Use of L-asparagine and N-phosphonacetyl-L-asparagine to investigate the linkage of catalysis and homotropic cooperativity in E. coli aspartate transcarbomoylase.
pubmed doi rcsb |
| molecule keywords |
Aspartate carbamoyltransferase catalytic chain
|
| source organism |
Escherichia coli
|
| molecule tags |
Transferase
|
| total genus |
27
|
| structure length |
153
|
| sequence length |
153
|
| chains with identical sequence |
D
|
| ec nomenclature | |
| pdb deposition date | 2006-10-12 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| B | PF01948 | PyrI | Aspartate carbamoyltransferase regulatory chain, allosteric domain |
| B | PF02748 | PyrI_C | Aspartate carbamoyltransferase regulatory chain, metal binding domain |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Mainly Beta | Roll | SH3 type barrels. | Aspartate carbamoyltransferase regulatory subunit, C-terminal domain | ||
| Alpha Beta | 2-Layer Sandwich | Alpha-Beta Plaits | Aspartate carbamoyltransferase regulatory subunit, N-terminal domain |
