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 |
186
|
sequence length |
498
|
structure length |
498
|
Chain Sequence |
SQLEHNIGLSIFEPVAKHRANRIVCTIGPSTQSVEALKNLMKSGMSVARMNFSHGSHEYHQTTINNVRAAAAELGLHIGIALDTKGPEIRTGLFKDGEVSFAPGDIVCVTTDPAYEKVGTKEKFYIDYPQLTNAVRPGGSIYVDDGVMTLRVVSKEDDRTLKCHVNNHHRLTDRRGINLPGCEVDLPAVSEKDRKDLEFGVAQGVDMIFASFIRTAEQVREVRAALGEKGKDILIISKIENHQGVQNIDSIIEASNGIMVARGDLGVEIPAEKVCVAQMCIISKCNVVGKPVICATQMLESMTSNPRPTRAEVSDVANAVLNGADCVMLSGETAKGKYPNEVVQYMARICVEAQSATHDTVMFNSIKNLQKIPMCPEEAVCSSAVASAFEVQAKAMLVLSNTGRSARLISKYRPNCPIICVTTRLQTCRQLNVTRSVVSVFYDAAKSGEDKDKEKRVKLGLDFAKKEKYASTGDVVVVVHADHSVKGYPNQTRLIYLP
|
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 |
Pyruvate kinases have an intrinsic and conserved decarboxylase activity.
pubmed doi rcsb |
molecule tags |
Transferase
|
source organism |
Trypanosoma brucei brucei
|
molecule keywords |
Pyruvate kinase 1
|
total genus |
186
|
structure length |
498
|
sequence length |
498
|
chains with identical sequence |
B
|
ec nomenclature |
ec
2.7.1.40: Pyruvate kinase. |
pdb deposition date | 2013-04-24 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00224 | PK | Pyruvate kinase, barrel domain |
A | PF02887 | PK_C | Pyruvate kinase, alpha/beta domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Phosphoenolpyruvate-binding domains | ||
Alpha Beta | 3-Layer(aba) Sandwich | Pyruvate Kinase; Chain: A, domain 1 | Pyruvate kinase, C-terminal domain |