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Crystal structure of endo-1,4-beta-xylanase-like protein from acremonium chrysogenum
Analyse Crystal structure of endo-1,4-beta-xylanase-like protein from acremonium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MRJ
- Type
- protein
- Length
- 612 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-xylanase
- EC
- 3.2.1.8
- UniProt
- A0A086SY89
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-xylanase (EC 3.2.1.8) | protein | 307 | 42% helix, 18% strand | A0A086SY89 |
| B | Beta-xylanase (EC 3.2.1.8) | protein | 305 | 41% helix, 19% strand | A0A086SY89 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.70 | 0.90 | 30 | SO4 |
| 2 | 516 | 0.70 | 0.80 | 74 | empty |
| 3 | 85 | 0.41 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1058 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5MRJ · Crystal structure of Endo-1,4-beta-xylanase-like protein from Acremonium chrysogenum · 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 A0A086SY89
- Elsewhere: RCSB PDB 5MRJ · PDBe 5MRJ · UniProt A0A086SY89
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