Research workbench
The xylanase ta from thermoascus aurantiacus utilizes arabinose decorations of xylan as significant substrate specificity determinants.
Analyse The xylanase ta from thermoascus aurantiacus utilizes arabinose decorations of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BNJ
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase
- EC
- 3.2.1.8
- UniProt
- P23360
- Ligands
- FER, XYP, AHR
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase (EC 3.2.1.8) | protein | 302 | 43% helix, 19% strand | P23360 |
Ligands and binding sites
- FER · 3-(4-hydroxy-3-methoxyphenyl)-2-propenoic acid · ligand
- XYP · beta-D-xylopyranose · sugar · 2 copies · chains A
- AHR · alpha-L-arabinofuranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.33 | 0.76 | 15 | XYP |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 2BNJ · The xylanase TA from Thermoascus aurantiacus utilizes arabinose decorations of xylan as… · the same entry in another collection · chain A against A, TM-score 1.00
- P23360 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P23360) · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P23360
- Elsewhere: RCSB PDB 2BNJ · PDBe 2BNJ · UniProt P23360
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