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 |
126
|
sequence length |
482
|
structure length |
445
|
Chain Sequence |
SNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESPVFQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDAACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLAPKISIFPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS
|
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 |
Mechanism of Coenzyme Binding to Human Methionine Synthase Reductase Revealed through the Crystal Structure of the FNR-like Module and Isothermal Titration Calorimetry
pubmed doi rcsb |
molecule tags |
Oxidoreductase
|
source organism |
Homo sapiens
|
molecule keywords |
Methionine synthase reductase
|
total genus |
126
|
structure length |
445
|
sequence length |
482
|
ec nomenclature |
ec
1.16.1.8: [Methionine synthase] reductase. |
pdb deposition date | 2007-08-02 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00175 | NAD_binding_1 | Oxidoreductase NAD-binding domain |
A | PF00667 | FAD_binding_1 | FAD binding domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Mainly Alpha | Up-down Bundle | NADPH-cytochrome p450 Reductase; Chain A, domain 3 | NADPH-cytochrome p450 Reductase; Chain A, domain 3 | ||
Mainly Beta | Beta Barrel | Elongation Factor Tu (Ef-tu); domain 3 | Translation factors | ||
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module |