MolNFT v1 · #112999 · protein
Crystal structure of anoxybacillus alpha-amylase provides insights into a new glycosyl hydrolase subclass
5A2C: “Crystal structure of anoxybacillus alpha-amylase provides insights into a new glycosyl hydrolase subclass”. X-ray diffraction, 2 ligands (GLC, CA), 1 pocket (best druggability 0.61). MolNFT v1 #112999 on GenesisL1: 3D structure…
- PDB
- 5A2C
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase
- EC
- 3.2.1.1
- UniProt
- I1VWH9
- Ligands
- GLC, CA
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-amylase (EC 3.2.1.1) | protein | 450 | 37% helix, 22% strand | I1VWH9 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- CA · Calcium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.61 | 0.82 | 22 | GLC |
Compared structures
- 5A2C · Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl… · 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 I1VWH9
- Elsewhere: RCSB PDB 5A2C · PDBe 5A2C · UniProt I1VWH9
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