Research workbench
High-resolution structures of xylanases from B. circulans and T. harzianum identify a new folding pattern and implications for the atomic basis of the catalysis
Analyse High-resolution structures of xylanases from B. circulans and T. harzianum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XND
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P48793
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 190 | — | P48793 |
Compared structures
- 1XND · High-resolution structures of xylanases from B. circulans and T. harzianum identify a new… · the same entry in another collection · chain A against A, TM-score 1.00
- P48793 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P48793) · a predicted model of the same protein · chain A 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 P48793
- Elsewhere: RCSB PDB 1XND · PDBe 1XND · UniProt P48793
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