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 |
156
|
sequence length |
444
|
structure length |
444
|
Chain Sequence |
RQGCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAIMDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHSTTSCFAPRVPDRLEELAVICANYDIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFNDSFIQEISKMYPGRASASPSLDVLISLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFRGFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVR
|
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 |
Structural basis for early-onset neurological disorders caused by mutations in human selenocysteine synthase.
pubmed doi rcsb |
| molecule tags |
Transferase
|
| source organism |
Homo sapiens
|
| molecule keywords |
O-phosphoseryl-tRNA(Sec) selenium transferase
|
| total genus |
156
|
| structure length |
444
|
| sequence length |
444
|
| chains with identical sequence |
B
|
| ec nomenclature |
ec
2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase. |
| pdb deposition date | 2015-04-17 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| A | PF05889 | SepSecS | O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Mainly Alpha | Orthogonal Bundle | Arc Repressor Mutant, subunit A | Arc Repressor Mutant, subunit A | ||
| Alpha Beta | 3-Layer(aba) Sandwich | Aspartate Aminotransferase; domain 2 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) | ||
| Alpha Beta | Alpha-Beta Complex | Aspartate Aminotransferase, domain 1 | Aspartate Aminotransferase, domain 1 |
