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 |
67
|
sequence length |
237
|
structure length |
237
|
Chain Sequence |
TLNTELPGRTNAFRIAEVRPQVNGIILKRLFKEGSDVKAGQQLYQIDPATYEADYQSAQANLASTQEQAQRYKLLVADQAVSKQQYADANAAYLQSKAAVEQARINLRYTKVLSPISGRIGRSAVTEGALVTNGQANAMATVQQLDPIYVDVTQPSTALLRLRRELASGQLERAGDNAAKVSLKLEDGSQYPLEGRLEFSEVSVDEGTGSVTIRAVFPNPNNELLPGMFVHAQLQEG
|
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 |
Multidrug resistance protein mexA
|
| publication title |
Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa
pubmed doi rcsb |
| source organism |
Pseudomonas aeruginosa
|
| molecule tags |
Membrane protein
|
| total genus |
67
|
| structure length |
237
|
| sequence length |
237
|
| chains with identical sequence |
B, C, D, E, F, G, H, I, J, K, L, M
|
| ec nomenclature | |
| pdb deposition date | 2004-04-09 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| A | PF00529 | HlyD | HlyD membrane-fusion protein of T1SS |
| A | PF16576 | HlyD_D23 | Barrel-sandwich domain of CusB or HlyD membrane-fusion |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Mainly Alpha | Orthogonal Bundle | Helix Hairpins | Helix hairpin bin | ||
| Mainly Beta | Beta Barrel | Elongation Factor Tu (Ef-tu); domain 3 | Elongation Factor Tu (Ef-tu); domain 3 | ||
| Mainly Beta | Beta Barrel | OB fold (Dihydrolipoamide Acetyltransferase, E2P) | OB fold (Dihydrolipoamide Acetyltransferase, E2P) |
