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Crystal structure of a GH131 beta-glucanase catalytic domain from Podospora anserina
Analyse Crystal structure of a GH131 beta-glucanase catalytic domain from Podospora… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LE3
- Type
- protein
- Length
- 983 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Podospora anserina
- Molecule
- Beta-glucanase
- UniProt
- J7K096
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · resolution 1.8 · 4 distinct chains · 5% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-glucanase | protein | 249 | 6% helix, 43% strand | J7K096 |
| B | Beta-glucanase | protein | 245 | 5% helix, 43% strand | J7K096 |
| C | Beta-glucanase | protein | 242 | 5% helix, 44% strand | J7K096 |
| D | Beta-glucanase | protein | 247 | 5% helix, 43% strand | J7K096 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.70 | 0.84 | 34 | empty |
| 2 | 164 | 0.56 | 0.81 | 32 | empty |
| 3 | 339 | 0.56 | 0.75 | 33 | empty |
| 4 | 101 | 0.50 | 0.82 | 24 | empty |
| 5 | 124 | 0.45 | 0.78 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 742 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 332 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 112 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4LE3 · Crystal structure of a GH131 beta-glucanase catalytic domain from podospora anserina · 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 J7K096
- Elsewhere: RCSB PDB 4LE3 · PDBe 4LE3 · UniProt J7K096
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