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 |
214
|
sequence length |
599
|
structure length |
599
|
Chain Sequence |
SHMAHQDALPRLPVPPLQQSLDYYLKALQPIVSEEEWAHTKQLVDEFQTSGGVGERLQKGLERRAKKMENWLSEWWLKTAYLQFRQPVVIYSSPGVILPKQDFVDLQGQLRFAAKLIEGVLDFKSMIDNETLPVEFLGGQPLCMNQYYQILSSCRVPGPKQDSVVNFLKSKRPPTHITVVHNYQFFELDVYHSDGTPLTSDQIFVQLEKIWNSSLQSNKEPVGILTSNHRNTWAKAYNNLIKDKVNRESVNSIQKSIFTVCLDKQVPRVSDDVYRNHVAGQMLHGGGSKFNSGNRWFDKTLQFIVAEDGSCGMVYEHAAAEGPPIVALVDHVMEYTKKPELVRSPMVPLPMPKKLRFNITPEIKNDIEKAKQNLSIMIQDLDIMMLTFHHFGKDFPKSEKLSPDAFIQVALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASIDSLAFVKGMGDSTVPEQQKVELLRKAVQAHRAYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFNLSTSQVPAKTDCVGFFGPVVPDGYGICYNPMEAHINFSVSAYNSCAETNAARMAHYLEKALLDMRTLLQNHPRAK
|
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.
| molecule tags |
Transferase
|
| molecule keywords |
Carnitine acetyltransferase
|
| publication title |
Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase
pubmed doi rcsb |
| source organism |
Mus musculus
|
| total genus |
214
|
| structure length |
599
|
| sequence length |
599
|
| ec nomenclature |
ec
2.3.1.7: Carnitine O-acetyltransferase. |
| pdb deposition date | 2004-05-10 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| A | PF00755 | Carn_acyltransf | Choline/Carnitine o-acyltransferase |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | 2-Layer Sandwich | Chloramphenicol Acetyltransferase | Chloramphenicol Acetyltransferase | ||
| Alpha Beta | 2-Layer Sandwich | Chloramphenicol Acetyltransferase | Chloramphenicol Acetyltransferase |
#chains in the Genus database with same CATH superfamily 2FW3 A; 2FY2 A; 1T1U A; 2H3U A; 2H4T A; 2H3W A; 1NM8 A; 1S5O A; 2RCU A; 1NDB A; 2DEB A; 2FY3 A; 1T7N A; 1T7O A; 2FYO A; 2H3P A; 1Q6X A; 1NDF A; 1NDI A; 2FY5 A; 2FY4 A; 4EPH A; 1T7Q A; 4EP9 A; 4EYW A; #chains in the Genus database with same CATH topology 2VSQ A; 2E1U A; 1CIA A; 1XL8 A; 2FW3 A; 1XMC A; 1C4T A; 2H3U A; 1NM8 A; 1EAE A; 1S5O A; 2FY3 A; 1T7N A; 5DUA A; 1NDF A; 2II5 A; 2II4 A; 5KJU A; 2XR7 A; 3B30 A; 1NDI A; 4JN5 A; 2CLA A; 4G0B A; 4EYW A; 3FP0 A; 5KJV A; 2XHG A; 3L60 A; 2FY2 A; 2RKT A; 2H4T A; 2H3W A; 1DPC A; 1NOC B; 2RCU A; 3CLA A; 4CLA A; 1DPB A; 1EAA A; 2E1T A; 2RKV A; 1Q6X A; 1EAD A; 2JGP A; 1CLA A; 1E2O A; 5FAN A; 3B2S A; 5T3E A; 4G22 A; 3MAE A; 4N72 A; 1EAB A; 4HVM A; 1SCZ A; 4G2M A; 2II3 A; 2DEB A; 5KJT A; 1T7O A; 1XMD A; 4EPH A; 1DPD A; 1EAF A; 1PD5 A; 1QCA A; 2BGH A; 5KJS A; 1Q9J A; 1T1U A; 5KJW A; 5DU9 A; 1Q23 A; 2I9D A; 1L5A A; 3U9B A; 4JN3 A; 1NDB A; 1XL7 A; 2FYO A; 2H3P A; 2ZBA A; 1EAC A; 4KEC A; 3FOT A; 3U9F A; 2FY5 A; 5FAL A; 2FY4 A; 2E1V A; 1T7Q A; 2IHW A; 4EP9 A; 4KE4 A; #chains in the Genus database with same CATH homology 5T3E A; 2XHG A; 2VSQ A; 1Q9J A; 2FW3 A; 2FY2 A; 1T1U A; 2H3U A; 5DU9 A; 2H4T A; 2H3W A; 1NM8 A; 4HVM A; 1L5A A; 1S5O A; 2RCU A; 4JN3 A; 1NDB A; 2DEB A; 2FY3 A; 1T7N A; 5DUA A; 1T7O A; 2FYO A; 2H3P A; 1Q6X A; 1NDF A; 2JGP A; 3FOT A; 1NDI A; 2FY5 A; 2FY4 A; 4JN5 A; 4EPH A; 1T7Q A; 4EP9 A; 4EYW A; 3FP0 A;
#similar chains in the Genus database (?% sequence similarity) ...loading similar chains, please wait... #similar chains, but unknotted ...loading similar chains, please wait... #similar chains in the pdb database (?% sequence similarity) ...loading similar chains, please wait...
