GL1X · GenesisL1 explorer

Research workbench

Structural and functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance

Analyse Structural and functional characterisation of three novel fungal amylases with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SAO
Type
protein
Length
438 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Amylase
Ligands
AC1, GLC, BGC, NAG, CA, SO4
Pockets
1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAmylaseprotein43835% helix, 19% strand—

Ligands and binding sites

  • AC1 · 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose · ligand · 2 copies · chains A
  • GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
  • BGC · beta-D-glucopyranose · sugar · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
  • CA · Calcium ion · metal · chains A
  • SO4 · Sulfate ion · ion · 6 copies · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11710.490.7725AC1, GLC

Modifications

Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 6SAO · Structural and functional characterisation of three novel fungal amylases with enhanced… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.