Table 2. Result of structural similarity search using the Dali server.
PDB IDa | Z score | RMSD (Å) | LALIb | Identity (%) | Protein namec | Organism | Activity | Family | Referenced |
---|---|---|---|---|---|---|---|---|---|
5mqr (A) | 31.4 | 2.6 | 459 | 19 | BT_1020 | Bacteroides thetaiotaomicron | β-L-Arabinofuranosidase | GH142 | [8] |
5ca4 (A) | 21.4 | 4.6 | 547 | 11 | YgjK | Escherichia coli | α-Glycosidase | GH63 | [30] |
2z07 (A) | 20.4 | 2.9 | 315 | 9 | TTHA0978 | Thermus thermophilus | (Uncharacterized) | GH63 | TBP |
3cih (A) | 20.3 | 4.3 | 441 | 10 | BT_1001 | Bacteroides thetaiotaomicron | α-L-Rhamnosidase | GH78 | [8] |
3w5m (A) | 19.4 | 3.8 | 427 | 13 | SaRha78A | Streptomyces avermitilis | α-L-Rhamnosidase | GH78 | [31] |
1v7v (A) | 19.4 | 4.2 | 581 | 9 | ChBP | Vibrio proteolyticus | Chitobiose phosphorylase | GH94 | [32] |
4wvb (A) | 19.0 | 2.9 | 315 | 9 | Tt8MGH | Thermus thermophilus | Mannosylglycerate hydrolase | GH63 | [33] |
6gsz (A) | 19.0 | 3.5 | 395 | 14 | α-Rha | Aspergillus terreus | α-L-Rhamnosidase | GH78 | [34] |
2jjb (B) | 19.0 | 3.4 | 341 | 12 | Tre37A | Escherichia coli | α,α-Trehalase | GH37 | [35] |
5ohz (C) | 18.7 | 3.7 | 331 | 8 | MhGgH | Mycolicibacterium hassiacum | Glucosylglycerate hydrolase | GH63 | [36] |
4zlf (A) | 18.1 | 4.5 | 469 | 10 | CBAP | Saccharophagus degradans | Cellobionic acid phosphorylase | GH94 | [37] |
3qde (A) | 18.1 | 4.2 | 585 | 10 | CtCBP | Clostridium thermocellum | Cellobiose phosphorylase | GH94 | [38] |
3afj (A) | 18.1 | 4.2 | 584 | 11 | CgCBP | Cellvibrio gilvus | Cellobiose phosphorylase | GH94 | [39] |
4j5t (A) | 18.0 | 3.7 | 444 | 9 | GluI | Saccharomyces cerevisiae | Processing α-glucosidase I | GH63 | [40] |
The whole HypBA2 structure including all domains were used.
aChain ID is shown in parentheses.
bNumber of aligned residues.
cTTHA0978 and Tt8MGH are the identical protein.
dTBP: to be published.