Research workbench
Five-domain alpha-amylase from bacillus stearothermophilus, maltose complex
Analyse Five-domain alpha-amylase from bacillus stearothermophilus, maltose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QHP
- Type
- protein
- Length
- 686 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase
- EC
- 3.2.1.133
- UniProt
- P19531
- Ligands
- GLC, CA, SO4
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-amylase (EC 3.2.1.133) | protein | 686 | 23% helix, 30% strand | P19531 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.69 | 0.86 | 37 | empty |
| 2 | 276 | 0.65 | 0.82 | 28 | GLC |
| 3 | 132 | 0.42 | 0.76 | 24 | empty |
| 4 | 61 | 0.34 | 0.77 | 15 | empty |
| 5 | 71 | 0.29 | 0.73 | 16 | empty |
Compared structures
- 1QHP · Five-domain alpha-amylase from bacillus stearothermophilus, maltose complex · the same entry in another collection · chain A against A, TM-score 1.00
- P19531 · AlphaFold monomer V2.0 prediction for maltogenic alpha-amylase (P19531) · a predicted model of the same protein · 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 P19531
- Elsewhere: RCSB PDB 1QHP · PDBe 1QHP · UniProt P19531
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