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 |
306
|
sequence length |
999
|
structure length |
986
|
Chain Sequence |
TIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKSVTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVDELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIFCDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFTEVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKISFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPRNDIDAAEFFEFCKKIASTLQFDVELDEKLIKEISYQARGDLVAMSAFLGGAVAQEVLKATTSKFYPLKQYFYFDSLESLPSSVTISEETCKPRGCRYDGQIAVFGSEFQEKIASLSTFLVGAGAIGCEMLKNWAMMGVATGESGHISVTDMDSIEKSNLNRQFLFRPRDVGKLKSECASTAVSIMNPSLTGKITSYQERVGPESEGIFGDEFFEKLSLVTNALDNVEARMYVDRRCVFFEKPLLESGTLGTKGNTQVVVPHLTESYGSSQDPPEKSFPICTLKNFPNRIEHTIAWARDLFEGLFKQPIDNVNMYLSSPNFLETSLKTSSNPREVLENIRDYLVTEKPLSFEECIMWARLQFDKFFNNNIQQLLFNFPKDSVTSTGQPFWSGPKRAPTPLSFDIHNREHFDFIVAAASLYAFNYGLKSETDPAIYERVLAGYNPPPFAPKSGIKIQVDKQELKSIADSLPPPSSLVGFRLTPAEFEKDDDSNHHIDFITAASNLRAMNYDITPADRFKTKFVAGKIVPAMCTSTAVVSGLVCLELVKLVDGKKKIEEYKNGFFNLAIGLFTFSDPIASPKMKVNGKEIDKIWDRYNLPDCTLQELIDYFQKEEGLEVTMLSSGVSLLYANFQPPKKLAERLPLKISELVEQITKKKLEPFRKHLVLEICCDDANGEDVEVPFICIKL
|
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-activating enzyme E1 1
|
| publication title |
Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester transfer.
pubmed doi rcsb |
| source organism |
Schizosaccharomyces pombe
|
| molecule tags |
Ligase
|
| total genus |
306
|
| structure length |
986
|
| sequence length |
999
|
| chains with identical sequence |
C
|
| ec nomenclature |
ec
6.2.1.45: E1 ubiquitin-activating enzyme. |
| pdb deposition date | 2012-12-19 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| A | PF00899 | ThiF | ThiF family |
| A | PF09358 | E1_UFD | Ubiquitin fold domain |
| A | PF10585 | UBA_e1_thiolCys | Ubiquitin-activating enzyme active site |
| A | PF16190 | E1_FCCH | Ubiquitin-activating enzyme E1 FCCH domain |
| A | PF16191 | E1_4HB | Ubiquitin-activating enzyme E1 four-helix bundle |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Mainly Alpha | Orthogonal Bundle | Arc Repressor Mutant, subunit A | Arc Repressor Mutant, subunit A | ||
| Mainly Beta | Beta Barrel | Elongation Factor Tu (Ef-tu); domain 3 | Elongation Factor Tu (Ef-tu); domain 3 | ||
| Alpha Beta | Roll | Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A | Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A | ||
| Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain | ||
| Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Rossmann fold | ||
| Alpha Beta | 3-Layer(bba) Sandwich | FAD/NAD(P)-binding domain | FAD/NAD(P)-binding domain |
