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 |
71
|
sequence length |
263
|
structure length |
258
|
Chain Sequence |
HMQAEILLTLKLQQKLFADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGAVLTRYGQRLIQLYDLLAQIQQKAFDVLSDDDALPLNSLLAAISRFSLQTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKVAITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEATSLQQGQNVTAYFNADSVIIATLC
|
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 high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds.
pubmed doi rcsb |
molecule tags |
Transcription
|
source organism |
Escherichia coli
|
molecule keywords |
PROTEIN (MODE)
|
total genus |
71
|
structure length |
258
|
sequence length |
263
|
chains with identical sequence |
B
|
ec nomenclature | |
pdb deposition date | 1999-02-12 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00126 | HTH_1 | Bacterial regulatory helix-turn-helix protein, lysR family |
A | PF03459 | TOBE | TOBE domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Mainly Alpha | Orthogonal Bundle | Arc Repressor Mutant, subunit A | Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain | ||
Mainly Beta | Beta Barrel | OB fold (Dihydrolipoamide Acetyltransferase, E2P) | OB fold (Dihydrolipoamide Acetyltransferase, E2P) | ||
Mainly Beta | Beta Barrel | OB fold (Dihydrolipoamide Acetyltransferase, E2P) | OB fold (Dihydrolipoamide Acetyltransferase, E2P) |