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 |
152
|
sequence length |
436
|
structure length |
436
|
Chain Sequence |
AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVSDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
|
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 keywords |
ENOLASE
|
| publication title |
Mechanism of enolase: the crystal structure of enolase-Mg2(+)-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-A resolution.
pubmed doi rcsb |
| source organism |
Saccharomyces cerevisiae
|
| molecule tags |
Carbon-oxygen lyase
|
| total genus |
152
|
| structure length |
436
|
| sequence length |
436
|
| ec nomenclature |
ec
4.2.1.11: Phosphopyruvate hydratase. |
| pdb deposition date | 1990-11-13 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| A | PF00113 | Enolase_C | Enolase, C-terminal TIM barrel domain |
| A | PF03952 | Enolase_N | Enolase, N-terminal domain |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Enolase-like C-terminal domain | ||
| Alpha Beta | 2-Layer Sandwich | Enolase-like; domain 1 | Enolase-like, N-terminal domain |
