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 |
105
|
sequence length |
381
|
structure length |
370
|
Chain Sequence |
IDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSPLSAMVSMVTKDNPGVVTCLDRHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLVASLAEPDFVKFSRPAQLHIGFQALHQFCAQHGRPPRPRNDEDAAELVALAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALE
|
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 |
Ubiquitin-like modifier-activating enzyme 1
|
publication title |
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1).
pubmed doi rcsb |
source organism |
Homo sapiens
|
molecule tags |
Ligase
|
total genus |
105
|
structure length |
370
|
sequence length |
381
|
chains with identical sequence |
B
|
ec nomenclature |
ec
6.2.1.45: E1 ubiquitin-activating enzyme. |
pdb deposition date | 2014-02-28 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF16190 | E1_FCCH | Ubiquitin-activating enzyme E1 FCCH domain |
A | PF16191 | E1_4HB | Ubiquitin-activating enzyme E1 four-helix bundle |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Mainly Beta | Beta Barrel | Elongation Factor Tu (Ef-tu); domain 3 | Elongation Factor Tu (Ef-tu); domain 3 | ||
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain |