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Taka-amylase

Analyse Taka-amylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YQ7
Type
protein
Length
952 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.58
Source
Aspergillus oryzae
Molecule
Alpha-amylase
EC
3.2.1.1
UniProt
A0A1S9DH83
Ligands
NAG, CA
Pockets
4 · best druggability 0.61

Structure

x-ray diffraction · resolution 1.58 · 1 distinct chain · 36% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlpha-amylase (EC 3.2.1.1)protein47636% helix, 21% strandA0A1S9DH83

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
  • CA · Calcium ion · metal · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13310.610.7829empty
23320.610.7825EDO
32930.580.7855empty
43280.550.7549empty

Interfaces

1 interface between chains.

  • A–B · 634 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6YQ7 · Taka-amylase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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