Research workbench
Crystal structure of apo beta-amylase from sweet potato
Analyse Crystal structure of apo beta-amylase from sweet potato in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WQS
- Type
- protein
- Length
- 496 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-amylase
- EC
- 3.2.1.2
- UniProt
- P10537
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-amylase (EC 3.2.1.2) | protein | 496 | 40% helix, 10% strand | P10537 |
Ligands and binding sites
- IPA · Isopropyl alcohol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 610 | 0.70 | 0.78 | 47 | IPA |
| 2 | 309 | 0.59 | 0.78 | 54 | empty |
| 3 | 79 | 0.44 | 0.80 | 16 | empty |
| 4 | 65 | 0.32 | 0.76 | 18 | empty |
| 5 | 55 | 0.31 | 0.76 | 13 | empty |
Compared structures
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 P10537
- Elsewhere: RCSB PDB 5WQS · PDBe 5WQS · UniProt P10537
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