Table III.
Comparison of the β-xylosidase modeled (WXyn43) with the crystallographic structures of two-domain β-xylosidases from family GH43
| Source | PDB code | Identities (%) | Positives (%) | Gaps (%) | Residues aligneda | Overall RMSD (Å)a |
|---|---|---|---|---|---|---|
| Weissella sp. strain. 92 | Model | 100 | 100 | 0 | 553 | 0 |
| Selenomonas ruminantium | 3C2U | 53 | 65 | 3 | 526 | 0.936 |
| Geobacillus stearothermophilus | 2EXI | 47 | 64 | 2 | 526 | 0.896 |
| Bacillus halodurans | 1YRZ | 47 | 61 | 5 | 513 | 1.137 |
| Bacillus subtilis subsp. subtilis | 1YIF | 49 | 64 | 3 | 488 | 0.788 |
| Clostridium acetobutylicum | 1Y7B | 51 | 67 | 2 | 501 | 0.784 |
3C2U, 2EXI and 1YRZ were used as templates for the hybrid model. Sequence similarities to WXyn43, and Cα-RMSD of the superimposed structures are given.
aThe overall RMSD was calculated from the residue aligned after superimposing the structures with a match alignment cutoff of 5.0 Å.