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 |
188
|
sequence length |
469
|
structure length |
467
|
Chain Sequence |
AQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKEMVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKGILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWT
|
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 |
Oxidoreductase
|
source organism |
Homo sapiens
|
publication title |
Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth.
pubmed doi rcsb |
molecule keywords |
6-phosphogluconate dehydrogenase, decarboxylating
|
total genus |
188
|
structure length |
467
|
sequence length |
469
|
ec nomenclature |
ec
1.1.1.44: Phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating). |
pdb deposition date | 2012-09-03 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00393 | 6PGD | 6-phosphogluconate dehydrogenase, C-terminal domain |
A | PF03446 | NAD_binding_2 | NAD binding domain of 6-phosphogluconate dehydrogenase |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Mainly Alpha | Orthogonal Bundle | N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2 | N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2 | ||
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain |