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 |
102
|
sequence length |
374
|
structure length |
374
|
Chain Sequence |
STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKCRVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGFDLLRSGESIRTILTF
|
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 |
Interdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode.
pubmed rcsb |
| molecule keywords |
APO-LIVER ALCOHOL DEHYDROGENASE
|
| source organism |
Equus caballus
|
| molecule tags |
Oxidoreductase (nad(a)-choh(d))
|
| total genus |
102
|
| structure length |
374
|
| sequence length |
374
|
| ec nomenclature |
ec
1.1.1.1: Alcohol dehydrogenase. |
| pdb deposition date | 1984-01-16 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| A | PF00107 | ADH_zinc_N | Zinc-binding dehydrogenase |
| A | PF08240 | ADH_N | Alcohol dehydrogenase GroES-like domain |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain | ||
| Alpha Beta | Alpha-Beta Complex | Quinone Oxidoreductase; Chain A, domain 1 | Medium-chain alcohol dehydrogenases, catalytic domain |
