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 |
192
|
sequence length |
539
|
structure length |
531
|
Chain Sequence |
RPRKYVFITGGVVSSLGKGILTSSLGALLRARGYRVTAIKIDPYVNVDAGTMRPYEHGEVFVTADGAETDLDIGHYERFLDMDLSRGNNLTTGQVYLSVIQKERRGEYLSQTVQVIPHITDEIKERIRKVAEEQKAEIVVVEVGGTVGDIESLPFLEAIRQFRFDEGEGNTLYLHLTLVPYLETSEEFKTKPTQHSVATLRGVGIQPDILVLRSARPVPEEVRRKVALFTNVRPGHVFSSPTVEHLYEVPLLLEEQGLGRAVERALGLEAVIPNLSFWQEAVRVLKHPERTVKIAIAGKYVDAYLSLLEALRHAGIKNRARVEVKWVDAESLADLEEAFRDVSGILVPGGFGVRGIEGKVRAAQYARERKIPYLGICLGLQIAVIEFARNVAGLKGANSTEFDPHTPHPVIDLMPEQLEVGGTMRLGDWPMRIKPGTLLHRLYGKEEVLERHRHRYEVNPLYVDGLERAGLVVSATTPGMRGRGAGLVEAIELKDHPFFLGLQSHPEFKSRPMRPSPPFVGFVEAALAYQE
|
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 |
Crystal Structures of CTP Synthetase Reveal ATP, UTP, and Glutamine Binding Sites
pubmed doi rcsb |
molecule tags |
Ligase
|
source organism |
Thermus thermophilus
|
molecule keywords |
CTP synthetase
|
total genus |
192
|
structure length |
531
|
sequence length |
539
|
ec nomenclature |
ec
6.3.4.2: CTP synthase (glutamine hydrolyzing). |
pdb deposition date | 2004-03-10 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00117 | GATase | Glutamine amidotransferase class-I |
A | PF06418 | CTP_synth_N | CTP synthase N-terminus |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | P-loop containing nucleotide triphosphate hydrolases | ||
Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Rossmann fold |