Research workbench
Family 13 alpha amylase in complex with acarbose
Analyse Family 13 alpha amylase in complex with acarbose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TAA
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Taka amylase
- EC
- 3.2.1.1
- UniProt
- P10529
- Ligands
- ABC, CA
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Taka amylase (EC 3.2.1.1) | protein | 476 | 35% helix, 21% strand | P10529 |
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 | 359 | 0.60 | 0.77 | 28 | ABC |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7TAA · Family 13 alpha amylase in complex with acarbose · 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 P10529
- Elsewhere: RCSB PDB 7TAA · PDBe 7TAA · UniProt P10529
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.