Xylanase from Bacillus circulans mutant E78Q/Y69A. Determined by X-ray diffraction at 1.5 Å resolution. Released 21 Aug 2024.
Explore 8QXZ in 3D Show helices and sheets RCSB PDB PDBe
8QXZ contains 6 α-helices and 22 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 1 |
| β-strand | 15-20 | 6 | 1 |
| β-strand | 25-31 | 7 | 1 |
| β-strand | 35-42 | 8 | 1 |
| α-helix | 49 | 1 | |
| β-strand | 50-73 | 24 | 1 |
| β-strand | 77-85 | 9 | 1 |
| β-strand | 93-100 | 8 | 1 |
| β-strand | 103-117 | 15 | 1 |
| β-strand | 120-132 | 13 | 1 |
| α-helix | 135-137 | 3 | |
| β-strand | 142-145 | 4 | 1 |
| α-helix | 146-155 | 10 | |
| β-strand | 163-184 | 22 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 2 |
| β-strand | 15-20 | 6 | 2 |
| β-strand | 25-31 | 7 | 2 |
| β-strand | 35-42 | 8 | 2 |
| β-strand | 50-73 | 24 | 2 |
| β-strand | 77-85 | 9 | 2 |
| β-strand | 93-100 | 8 | 2 |
| β-strand | 103-117 | 15 | 2 |
| β-strand | 120-132 | 13 | 2 |
| α-helix | 135-137 | 3 | |
| β-strand | 142-145 | 4 | 2 |
| α-helix | 146-155 | 10 | |
| α-helix | 159-161 | 3 | |
| β-strand | 163-184 | 22 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endo-1,4-beta-xylanase | A, B | protein | 185 | Niallia circulans subsp. circulans | P09850 (AlphaFold model) |
>8QXZ_1 Endo-1,4-beta-xylanase (chains A, B) ASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTINYNAGVWAP NGNGYLTLAGWTRSPLIQYYVVDSWGTYRPTGTYKGTVKSDGGTYDIYTTTRYNAPSIDG DRTTFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNLGSNWAYQVMATEGYQSSGSS NVTVW
| ID | Name | Formula | Copies |
|---|---|---|---|
| BTB | 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol | C8 H19 N O5 | 2 |
| ZN | Zinc ion | Zn | 2 |
Water and common crystallization additives (GOL, PEG) are not listed.
Bimodal substrate binding in the active site of the glycosidase BcX. Saberi, M., Chikunova, A., Ben Bdira, F. et al. FEBS J (2024) 291:4222-4239. DOI 10.1111/febs.17251 · PubMed
Other PDB entries of the same protein (UniProt P09850 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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