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 |
231
|
sequence length |
733
|
structure length |
728
|
Chain Sequence |
LQLRVNEKLDVENILKDLDKYTPKRRGWTWRQPAENLQMGPFIYKDASTPLENSVALPSAKYFGDIDPQPLPVITTEIASGRFEDDIRRMRMAAWHGADHIMVIRTAGQSHYDGLIEGTPQGIGGVPITRKQVRAQRKALDLIEEEVGRPINYHSYVSGVAGPDIAVMFAEEGVNGAHQDPQYNVLYRNINMIRSFIDACESKTIMAWADMAQIDGAHNANATAREAWKVMPELMVQHALNSIFSLKVGMKKSNICLSTVPPTAPPAPSMYLDLPYAVALREMFEGYRMRAQMNTKYMEASTREATVTHVLNLLISKLTRADIQSTITPDEGRNVPWHIYNIEACDTAKQALIGMDGLMDMVQLKREGVLGDTVRELKERAVLFMEEIIEAGGYFNAVEQGFFVDSGYYPERNGDGIARQINGGIGAGTVFERDEDYMAPVTAHFGYNNVKQYDEALVSEPSKLIDGCTLEVPEKIVYIDELDENDNVNVRMEETKEFRSMIKPEVEWQADGTVLLTMFLPTSKRVAEFAAIEFAKKMNLEEVEVINREVMQEAEGTRIELKGRVPFSIDINSLVIPPILSEDEIREDIEKTPLKIVAATVGEDEHSVGLREVIDIKHGGIEKYGVEVHYLGTSVPVEKLVDAAIELKADAILASTIISHDDIHYKNMKRIHELAVEKGIRDKIMIGCGGTQVTPEVAVKQGVDAGFGRGSKGIHVATFLVKKRREMR
|
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 |
Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase.
pubmed doi rcsb |
molecule tags |
Metal binding protein
|
source organism |
Clostridium sticklandii
|
molecule keywords |
D-ornithine aminomutase E component
|
total genus |
231
|
structure length |
728
|
sequence length |
733
|
chains with identical sequence |
B, C, D
|
ec nomenclature |
ec
5.4.3.5: D-ornithine 4,5-aminomutase. |
pdb deposition date | 2009-11-14 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF02310 | B12-binding | B12 binding domain |
A | PF09043 | Lys-AminoMut_A | D-Lysine 5,6-aminomutase TIM-barrel domain of alpha subunit |
A | PF16554 | OAM_dimer | Dimerisation domain of d-ornithine 4,5-aminomutase |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Alpha Beta | Alpha-Beta Barrel | TIM Barrel | D-Lysine 5,6-aminomutase alpha subunit | ||
Alpha Beta | 2-Layer Sandwich | Defensin A-like | D-lysine 5,6-aminomutase beta subunit KamE, N-terminal domain | ||
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Cobalamin-binding domain |