Research workbench
Alkaline alpha-amylase amyk from bacillus sp. ksm-1378
Analyse Alkaline alpha-amylase amyk from bacillus sp. ksm-1378 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DIE
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amylase
- EC
- 3.2.1.1
- UniProt
- O82839
- Ligands
- CA, NA
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amylase (EC 3.2.1.1) | protein | 481 | 27% helix, 25% strand | O82839 |
Ligands and binding sites
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 | 0.55 | 0.78 | 24 | empty |
Compared structures
- 2DIE · Alkaline alpha-amylase AmyK from Bacillus sp. KSM-1378 · 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 O82839
- Elsewhere: RCSB PDB 2DIE · PDBe 2DIE · UniProt O82839
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