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Role of mobile loop in the mechanism of human salivary amylase

Analyse Role of mobile loop in the mechanism of human salivary amylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1JXJ
Type
protein
Length
496 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-amylase, salivary
EC
3.2.1.1
UniProt
P04745
Ligands
CA, CL
Pockets
3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-amylase, salivary (EC 3.2.1.1)protein49628% helix, 24% strandP04745

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
13670.610.7735empty
2800.340.7525empty
3690.320.7514empty

Modifications

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

Compared structures

  • 1JXJ · Role of mobile loop in the mechanism of human salivary amylase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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