Research workbench
Crystal structure of alpha-amylase II (tvaii) from thermoactinomyces vulgaris R-47 and beta-cyclodextrin complex
Analyse Crystal structure of alpha-amylase II (tvaii) from thermoactinomyces vulgaris… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G1Y
- Type
- protein
- Length
- 1,170 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase II
- EC
- 3.2.1.135
- UniProt
- Q08751
- Ligands
- GLC
- Pockets
- 12 · best druggability 0.90
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-amylase II (EC 3.2.1.135) | protein | 585 | 28% helix, 26% strand | Q08751 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 14 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1137 | 0.90 | 0.91 | 126 | empty |
| 2 | 186 | 0.53 | 0.78 | 31 | GLC |
| 3 | 174 | 0.52 | 0.79 | 23 | empty |
| 4 | 176 | 0.50 | 0.77 | 30 | GLC |
| 5 | 112 | 0.48 | 0.81 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 2312 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 1G1Y · Crystal structure of alpha-amylase II (tvaii) from thermoactinomyces vulgaris R-47 and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q08751 · AlphaFold monomer V2.0 prediction for neopullulanase 2 (Q08751) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q08751
- Elsewhere: RCSB PDB 1G1Y · PDBe 1G1Y · UniProt Q08751
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.