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Crystal structure of GSDMA3

Analyse Crystal structure of GSDMA3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5B5R
Type
protein
Length
409 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gasdermin-A3
UniProt
Q5Y4Y6
Pockets
8 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGasdermin-A3protein40943% helix, 21% strandQ5Y4Y6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13510.650.8045empty
23060.610.7938empty
32630.510.7538empty
41360.370.7323empty
5740.330.7512empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 5B5R · Crystal structure of GSDMA3 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5Y4Y6 · AlphaFold monomer V2.0 prediction for gasdermin-A3 (Q5Y4Y6) · a predicted model of the same protein · chain A against A, TM-score 0.90

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