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 |
128
|
sequence length |
453
|
structure length |
433
|
Chain Sequence |
EESDQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILDEYWQNHPELHDIPIYYASSLAKKCMAVYQTYVNANNPFVFKHISNLKSMDHFDDIGPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEITTMSGQKLPLKMSVDYISFSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYEDNDEVHIEVHNPRNTEAVTLNFR
|
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 |
Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.
pubmed doi rcsb |
molecule tags |
Hydrolase, rna binding protein
|
source organism |
Homo sapiens
|
molecule keywords |
Cleavage and polyadenylation specificity factor 73 kDa subun
|
total genus |
128
|
structure length |
433
|
sequence length |
453
|
ec nomenclature | |
pdb deposition date | 2006-08-31 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00753 | Lactamase_B | Metallo-beta-lactamase superfamily |
A | PF07521 | RMMBL | Zn-dependent metallo-hydrolase RNA specificity domain |
A | PF10996 | Beta-Casp | Beta-Casp domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Rossmann fold | ||
Alpha Beta | 4-Layer Sandwich | Metallo-beta-lactamase; Chain A | Ribonuclease Z/Hydroxyacylglutathione hydrolase-like |