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 |
174
|
sequence length |
457
|
structure length |
456
|
Chain Sequence |
MDIIIKNGTIVTADGISRADLGIKDGKITQIGGALGPAERTIDAAGRYVFPGGIDVHTHVETVSFNTQSADTFATATVAAACGGTTTIVDFCQQDRGHSLAEAVAKWDGMAGGKSAIDYGYHIIVLDPTDSVIEELEVLPDLGITSFVFMAYRGMNMIDDVTLLKTLDKAVKTGSLVMVHAENGDAADYLRDKFVAEGKTAPIYHALSRPPRVEAEATARALALAEIVNAPIYIVHVTCEESLEEVMRAKSRGVRALAETCTHYLYLTKEDLERPDFEGAKYVFTPPARAKKDHDVLWNALRNGVFETVSSDHCSWLFKGHKDRGRNDFRAIPNGAPGVEERLMMVYQGVNEGRISLTQFVELVATRPAKVFGMFPQKGTIAVGSDADIVLWDPEAEMVIEQTAMHNAMDYSSYEGHKVKGVPKTVLLRGKVIVDEGSYVGEPTDGKFLKRRKYKQ
|
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 Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability.
pubmed doi rcsb |
molecule tags |
Hydrolase
|
source organism |
Ralstonia pickettii
|
molecule keywords |
D-hydantoinase
|
total genus |
174
|
structure length |
456
|
sequence length |
457
|
chains with identical sequence |
B, C, D
|
ec nomenclature |
ec
3.5.2.2: Dihydropyrimidinase. |
pdb deposition date | 2002-12-14 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00449 | Urease_alpha | Urease alpha-subunit, N-terminal domain |
A | PF01979 | Amidohydro_1 | Amidohydrolase family |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Mainly Beta | Roll | Urease, subunit C; domain 1 | Urease, subunit C, domain 1 | ||
Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Metal-dependent hydrolases |