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2.0 ångström structure of intact alpha-1-antitrypsin: a canonical template for active serpins

Analyse 2.0 ångström structure of intact alpha-1-antitrypsin: a canonical template for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QLP
Type
protein
Length
372 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-1-antitrypsin
UniProt
P01009
Pockets
4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-1-antitrypsinprotein37229% helix, 30% strandP01009

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.610.8324empty
2740.530.8624empty
3930.370.7516empty
4940.360.7423empty

Compared structures

  • 1QLP · 2.0 ångström structure of intact alpha-1-antitrypsin: a canonical template for active… · 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 0.99

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