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Crystal structure of an aromatic mutant (W6A) of an alkali thermostable GH10 xylanase from bacillus sp. ng-27
Analyse Crystal structure of an aromatic mutant (W6A) of an alkali thermostable GH10… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XC0
- Type
- protein
- Length
- 707 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-xylanase
- EC
- 3.2.1.8
- UniProt
- O30700
- Ligands
- MG, NA
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-xylanase (EC 3.2.1.8) | protein | 353 | 44% helix, 17% strand | O30700 |
| B | Beta-xylanase (EC 3.2.1.8) | protein | 354 | 42% helix, 17% strand | O30700 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 633 | 0.78 | 0.83 | 75 | empty |
| 2 | 140 | 0.58 | 0.83 | 32 | empty |
| 3 | 150 | 0.51 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 733 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5XC0 · Crystal structure of an aromatic mutant (W6A) of an alkali thermostable GH10 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
- Every structure of UniProt O30700
- Elsewhere: RCSB PDB 5XC0 · PDBe 5XC0 · UniProt O30700
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