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Three-dimensional structure of a variant `termamyl-like' geobacillus stearothermophilus alpha-amylase at 1.9 a resolution

Analyse Three-dimensional structure of a variant `termamyl-like' geobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4UZU
Type
protein
Length
479 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-amylase
EC
3.2.1.1
UniProt
P06279
Ligands
GLY, CA, NA, CL
Pockets
2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-amylase (EC 3.2.1.1)protein47927% helix, 27% strandP06279

Ligands and binding sites

  • GLY · Glycine · ligand · 2 copies · chains A
  • CA · Calcium ion · metal · 3 copies · chains A
  • NA · Sodium ion · metal · 3 copies · chains A
  • CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11610.500.7825NA
2550.400.8118empty

Compared structures

  • 4UZU · Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus… · the same entry in another collection · chain A against A, TM-score 1.00
  • P06279 · AlphaFold monomer V2.0 prediction for alpha-amylase (P06279) · a predicted model of the same protein · chain A against A, TM-score 0.99

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