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 |
203
|
sequence length |
556
|
structure length |
556
|
Chain Sequence |
b'MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREAPRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKRQPWCVEIPRLAEQAMQAVIARRDAFGEAQLAHRICDYLPEQGQLFVGNSLVVRLIDALSQLPAGYPVYSNAGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNGGQIFSLLPTPQSERERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVNDTDGAQTLQQLLAQVSHL'
|
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 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxyla
|
| molecule tags |
Transferase
|
| source organism |
Escherichia coli k12
|
| publication title |
Two active site arginines are critical determinants of substrate binding and catalysis in MenD, a thiamine-dependent enzyme in menaquinone biosynthesis.
pubmed doi rcsb |
| total genus |
203
|
| structure length |
556
|
| sequence length |
556
|
| chains with identical sequence |
B, C, D, E, F, G, H
|
| ec nomenclature |
ec
2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid |
| pdb deposition date | 2015-11-02 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| A | PF02775 | TPP_enzyme_C | Thiamine pyrophosphate enzyme, C-terminal TPP binding domain |
| A | PF02776 | TPP_enzyme_N | Thiamine pyrophosphate enzyme, N-terminal TPP binding domain |
| A | PF16582 | TPP_enzyme_M_2 | Middle domain of thiamine pyrophosphate |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Rossmann fold | ||
| Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Rossmann fold | ||
| Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | TPP-binding domain |
