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Crystal structure of pullulanase type I from Bacillus subtilis str. 168
Analyse Crystal structure of pullulanase type I from Bacillus subtilis str. 168 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E8Y
- Type
- protein
- Length
- 1,424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.11
- Source
- Bacillus subtilis
- Molecule
- AmyX protein
- EC
- 3.2.1.41
- UniProt
- O34587
- Ligands
- CA
- Pockets
- 17 · best druggability 0.76
Structure
x-ray diffraction · resolution 2.11 · 1 distinct chain · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | AmyX protein (EC 3.2.1.41) | protein | 712 | 29% helix, 28% strand | O34587 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1013 | 0.76 | 0.78 | 74 | empty |
| 2 | 50 | 0.66 | 0.96 | 21 | empty |
| 3 | 55 | 0.65 | 0.95 | 19 | GOL |
| 4 | 223 | 0.55 | 0.78 | 31 | empty |
| 5 | 181 | 0.52 | 0.78 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 495 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2E8Y · Crystal structure of pullulanase type I from bacillus subtilis str. 168 · 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 O34587
- Elsewhere: RCSB PDB 2E8Y · PDBe 2E8Y · UniProt O34587
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