Research workbench
A mutant of Axe2 (R55A), and acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus
Analyse A mutant of Axe2 (R55A), and acetyl-xylooligosaccharide esterase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OAO
- Type
- protein
- Length
- 438 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.05
- Source
- Geobacillus stearothermophilus
- Molecule
- Acetyl xylan esterase
- UniProt
- Q09LX1
- Ligands
- CL
- Pockets
- 5 · best druggability 0.45
Structure
x-ray diffraction · resolution 2.05 · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetyl xylan esterase | protein | 219 | 51% helix, 11% strand | Q09LX1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.45 | 0.78 | 17 | empty |
| 2 | 130 | 0.45 | 0.77 | 22 | GOL |
| 3 | 100 | 0.43 | 0.78 | 17 | empty |
| 4 | 98 | 0.39 | 0.76 | 22 | empty |
| 5 | 72 | 0.30 | 0.73 | 18 | GOL |
Interfaces
1 interface between chains.
- A–B · 1206 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4OAO · A mutant of AXE2 (R55A), and acetyl-xylooligosaccharide esterase from geobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q09LX1 · AlphaFold monomer V2.0 prediction for acetylxylan esterase (Q09LX1) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q09LX1
- Elsewhere: RCSB PDB 4OAO · PDBe 4OAO · UniProt Q09LX1
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