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 |
109
|
sequence length |
333
|
structure length |
333
|
Chain Sequence |
MIRWGLIGASTIAREWVIGAIRAAGGEVVSVMSSSAERGEAYAAENGIAKAVTSVDDLVGDPDVDAVYISTTNELHHGQALAAIRAGKHVLCEKPLAMNLNDGCEMVLKACEAGVVLGTNHHLRNAATHRAMREAIAAGRIGRPIAARVFHAVYLPPHLQGWRLDKPEAGGGVILDITVHDADTLRFVLNDDPIEAVAISHSAGMGKEGLEDGVMGVLRFRSGVIAQFHDAFTTKFAETGLEVHGTAGSLIGRNVMTQRPVGTVVLRNEEGESELPLDHRNLYETAIAAFHSAIGGNGRPSASGEDGVWSLATGLAVVKAAATGGAVEIETGL
|
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 |
The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation.
pubmed doi rcsb |
molecule tags |
Oxidoreductase
|
source organism |
Sinorhizobium meliloti
|
molecule keywords |
1,5-anhydro-D-fructose reductase
|
total genus |
109
|
structure length |
333
|
sequence length |
333
|
ec nomenclature |
ec
1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming). |
pdb deposition date | 2013-05-11 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF01408 | GFO_IDH_MocA | Oxidoreductase family, NAD-binding Rossmann fold |
A | PF02894 | GFO_IDH_MocA_C | Oxidoreductase family, C-terminal alpha/beta domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Alpha Beta | 2-Layer Sandwich | Dihydrodipicolinate Reductase; domain 2 | Dihydrodipicolinate Reductase; domain 2 | ||
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain |