Research workbench
Crystal structure of alpha-amylase from H.ORENII
Analyse Crystal structure of alpha-amylase from H.ORENII in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WZA
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase a
- EC
- 3.2.1.1
- UniProt
- Q8GPL8
- Ligands
- CA
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-amylase a (EC 3.2.1.1) | protein | 488 | 31% helix, 20% strand | Q8GPL8 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.67 | 0.77 | 48 | empty |
| 2 | 94 | 0.45 | 0.79 | 28 | empty |
| 3 | 63 | 0.30 | 0.74 | 16 | empty |
Compared structures
- 1WZA · Crystal structure of alpha-amylase from H.orenii · 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 Q8GPL8
- Elsewhere: RCSB PDB 1WZA · PDBe 1WZA · UniProt Q8GPL8
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