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Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A

Analyse Native structure of chimaeric amylase from B. amyloliquefaciens and B.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1E43
Type
protein
Length
483 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-amylase
EC
3.2.1.1
UniProt
P00692, P06278
Ligands
CA, NA
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-amylase (EC 3.2.1.1)protein48326% helix, 25% strandP00692, P06278

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains A
  • NA · Sodium ion · metal · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.530.7925empty
2600.340.7713empty

Compared structures

  • 1E43 · Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00692 · AlphaFold monomer V2.0 prediction for alpha-amylase (P00692) · a predicted model of the same protein · chain A against A, TM-score 1.00
  • P06278 · AlphaFold monomer V2.0 prediction for alpha-amylase (P06278) · a predicted model of the same protein · chain A against A, TM-score 0.99

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