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The structure of human pancreatic alpha-amylase at 1.8 ångströms resolution and comparisons with related enzymes

Analyse The structure of human pancreatic alpha-amylase at 1.8 ångströms resolution and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HNY
Type
protein
Length
496 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Human pancreatic alpha-amylase
EC
3.2.1.1
UniProt
P04746
Ligands
CA, CL
Pockets
3 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHuman pancreatic alpha-amylase (EC 3.2.1.1)protein49627% helix, 24% strandP04746

Ligands and binding sites

  • CA · Calcium ion · metal · chains A
  • CL · Chloride ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12950.580.7725empty
2760.330.7520empty
3510.280.7513empty

Modifications

Observed in the structure: 5 disulfide, 1 modified (disulfide, cyclization).

Compared structures

  • 1HNY · The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and… · the same entry in another collection · chain A against A, TM-score 1.00
  • P04746 · AlphaFold monomer V2.0 prediction for pancreatic alpha-amylase (P04746) · a predicted model of the same protein · chain A against A, TM-score 1.00

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