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 |
180
|
sequence length |
637
|
structure length |
600
|
Chain Sequence |
HMSSLQRASVSFNKPGHIPFGAVQGYAPGGVPAYSNKHDHYFSGERNIEDNIFFGFKYQCVEFARRWLLVRKGLLLPDVNWACHIFQLKEVRDAATTESFAVLQVRNGTTTKPEADALLVYPSTDANPVGHVGTITEVGDDYVCVADQNYRFHKWESSCAYKLKLDHRDGIWTIIDDIDADEIEIPLGWLTFPGRANRPEGAPPVALHPSLHFKEPPKPYLLRRNFLPTESKANWLDMNNPAERLFVEEFGMVVSYYESNHEFHLRCVAYGTQLHAIFMEATAQVIESDEKLRLFAIPEEFWPRIRHSWKYQQTYISGRFDFAFNNETGEVKCFEYNADSASTLLECGLIQQKWAESVGLDKQDTRGSGFAVERNLKMAWANSGATGRVHFCVDEEREEQYTALYCMQAAEAVGLEGKLCILFDEFRFDDNGHVVDSDGVRVRNVWKTWMWESAITDYYAAREERGENWKPSPKDKVRLCDLLLGDDWEILYFEPMWKVIPSNKAILPMIYHNHPEHPAILKAEYELTDELRKHGYAKKPIVNMIYQQLFELKKQDDYYAIIGGWMIGDAFSGTGIREDKSVITGVDSPFAAVRIKTDKL
|
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 |
Leishmania Trypanothione Synthetase-Amidase Structure Reveals a Basis for Regulation of Conflicting Synthetic and Hydrolytic Activities.
pubmed doi rcsb |
molecule tags |
Ligase
|
source organism |
Leishmania major
|
molecule keywords |
TRYPANOTHIONE SYNTHETASE
|
total genus |
180
|
structure length |
600
|
sequence length |
637
|
chains with identical sequence |
B
|
ec nomenclature |
ec
6.3.1.9: Trypanothione synthase. |
pdb deposition date | 2008-03-03 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF03738 | GSP_synth | Glutathionylspermidine synthase preATP-grasp |
A | PF05257 | CHAP | CHAP domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Alpha Beta | Alpha-Beta Complex | endopeptidase fold (from Nostoc punctiforme) | endopeptidase domain like (from Nostoc punctiforme) |
#chains in the Genus database with same CATH superfamily 2IF6 A; 4FGI A; 4EQA A; 4HPE A; 4FGE A; 2FG0 A; 2IOB A; 4JXB A; 3PBC A; 4LJ1 A; 4CT3 A; 3VPJ A; 2LRJ A; 4HZB A; 3PVQ A; 4FGD A; 4CGK A; 3NPF A; 4R0K A; 4Q4T A; 2K3A A; 3I86 A; 4HZ9 A; 4OLK A; 3O98 A; 3H41 A; 3PBI A; 3S0Q A; 4F4M A; 2XIV A; 2EVR A; 4F0W A; 3A2Z A; 3NE0 A; 2IO7 A; 2IO8 A; 3GT2 A; 4EQ8 A; 3KW0 A; 2K1G A; 4EOB A; 2VPS A; 2VOB A; 4F0V A; 2HBW A; 2IO9 A; 4FDY A; 4FQB A; 4CSH A; 4Q4N A; 3A30 A; 2VPM A; 3M1U A; 4FQA A; 3VPI A; 4Q4G X; 2IOA A; 3A2Y A; #chains in the Genus database with same CATH topology 2IF6 A; 4FGI A; 4EQA A; 4HPE A; 4FGE A; 2FG0 A; 2IOB A; 4JXB A; 3PBC A; 4LJ1 A; 4CT3 A; 3VPJ A; 2LRJ A; 4HZB A; 3PVQ A; 4FGD A; 4CGK A; 3NPF A; 4HFF A; 2WP7 A; 4Q4T A; 4R0K A; 2K3A A; 3I86 A; 4HZ9 A; 4J32 A; 3O98 A; 4J30 A; 4OLK A; 3H41 A; 3PBI A; 3S0Q A; 4F4M A; 2XIV A; 4HFL A; 2EVR A; 4F0W A; 3A2Z A; 3NE0 A; 2IO7 A; 2IO8 A; 3GT2 A; 4EQ8 A; 3KW0 A; 2K1G A; 4EOB A; 2VPS A; 2VOB A; 4F0V A; 2HBW A; 2IO9 A; 4JUR A; 4FDY A; 4FQB A; 4CSH A; 4HFK A; 4Q4N A; 3A30 A; 2VPM A; 3M1U A; 4FQA A; 3EBQ A; 3VPI A; 4Q4G X; 2IOA A; 3A2Y A; #chains in the Genus database with same CATH homology 2IF6 A; 4FGI A; 4EQA A; 4HPE A; 4FGE A; 2FG0 A; 2IOB A; 4JXB A; 3PBC A; 4LJ1 A; 4CT3 A; 3VPJ A; 2LRJ A; 4HZB A; 3PVQ A; 4FGD A; 4CGK A; 3NPF A; 4R0K A; 4Q4T A; 2K3A A; 3I86 A; 4HZ9 A; 4OLK A; 3O98 A; 3H41 A; 3PBI A; 3S0Q A; 4F4M A; 2XIV A; 2EVR A; 4F0W A; 3A2Z A; 3NE0 A; 2IO7 A; 2IO8 A; 3GT2 A; 4EQ8 A; 3KW0 A; 2K1G A; 4EOB A; 2VPS A; 2VOB A; 4F0V A; 2HBW A; 2IO9 A; 4FDY A; 4FQB A; 4CSH A; 4Q4N A; 3A30 A; 2VPM A; 3M1U A; 4FQA A; 3VPI A; 4Q4G X; 2IOA A; 3A2Y A;
#similar chains in the Genus database (?% sequence similarity) ...loading similar chains, please wait... #similar chains, but unknotted ...loading similar chains, please wait... #similar chains in the pdb database (?% sequence similarity) ...loading similar chains, please wait...