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Crystal structure of endo-1,4-beta-xylanase from cellulomonas flavigena
Analyse Crystal structure of endo-1,4-beta-xylanase from cellulomonas flavigena in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M0K
- Type
- protein
- Length
- 598 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-xylanase
- EC
- 3.2.1.8
- UniProt
- D5UH90
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-xylanase (EC 3.2.1.8) | protein | 299 | 42% helix, 20% strand | D5UH90 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 930 | 0.69 | 0.74 | 88 | empty |
| 2 | 185 | 0.51 | 0.78 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 409 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5M0K · CRYSTAL STRUCTURE of endo-1,4-beta-xylanase from Cellulomonas flavigena · 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 D5UH90
- Elsewhere: RCSB PDB 5M0K · PDBe 5M0K · UniProt D5UH90
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