Research workbench
Crystal structure of calcium-free alpha-amylase from bacillus sp. strain ksm-K38 (AMYK38)
Analyse Crystal structure of calcium-free alpha-amylase from bacillus sp. strain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UD2
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amylase
- EC
- 3.2.1.1
- UniProt
- Q93I48
- Ligands
- NA
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amylase (EC 3.2.1.1) | protein | 480 | 28% helix, 26% strand | Q93I48 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.52 | 0.79 | 23 | empty |
| 2 | 63 | 0.30 | 0.75 | 13 | empty |
Compared structures
- 1UD2 · Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) · 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 Q93I48
- Elsewhere: RCSB PDB 1UD2 · PDBe 1UD2 · UniProt Q93I48
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.