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Alpha-1-antitrypsin QUEEN'S (LYS154ASN) variant

Analyse Alpha-1-antitrypsin QUEEN'S (LYS154ASN) variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IAY
Type
protein
Length
368 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-1-antitrypsin
UniProt
P01009
Ligands
GLY
Pockets
3 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-1-antitrypsinprotein36830% helix, 32% strandP01009

Ligands and binding sites

  • GLY · Glycine · ligand · 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
1900.580.8723empty
2500.340.7913empty
3800.320.7418empty

Compared structures

  • 6IAY · Alpha-1-antitrypsin Queen's (Lys154Asn) variant · the same entry in another collection · chain A against A, TM-score 1.00
  • P01009 · AlphaFold monomer V2.0 prediction for alpha-1-antitrypsin (P01009) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

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