Research workbench
Crystal structure, at 2.6 ångströms resolution, of the streptomyces lividans xylanase a, a member of the F family of beta-1,4-D-glycanses
Analyse Crystal structure, at 2.6 ångströms resolution, of the streptomyces lividans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XAS
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1,4-beta-D-xylan xylanohydrolase
- EC
- 3.2.1.8
- UniProt
- P26514
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1,4-beta-D-xylan xylanohydrolase (EC 3.2.1.8) | protein | 295 | 0% helix, 0% strand | P26514 |
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 | 75 | 0.33 | 0.73 | 22 | empty |
Compared structures
- 1XAS · Crystal structure, at 2.6 ångströms resolution, of the streptomyces lividans xylanase a… · the same entry in another collection · chain A against A, TM-score 1.00
- P26514 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase a (P26514) · 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 P26514
- Elsewhere: RCSB PDB 1XAS · PDBe 1XAS · UniProt P26514
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