Research workbench
Thermostable mutant of environmentally isolated GH11 xylanase
Analyse Thermostable mutant of environmentally isolated GH11 xylanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VUL
- Type
- protein
- Length
- 193 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GH11 xylanase
- EC
- 3.2.1.8
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GH11 xylanase (EC 3.2.1.8) | protein | 193 | 5% helix, 62% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
- 12P · Dodecaethylene glycol · additive · 3 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 161 | 0.50 | 0.78 | 33 | 12P |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2VUL · Thermostable mutant of ENVIRONMENTALLY ISOLATED GH11 XYLANASE · the same entry in another collection · 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
- Elsewhere: RCSB PDB 2VUL · PDBe 2VUL
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