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Crystal structure of lgg-1 complexed with a weel peptide

Analyse Crystal structure of lgg-1 complexed with a weel peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5AZF
Type
protein
Length
246 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein lgg-1; Peptide from autophagy-related protein 19
UniProt
Q09490, P35193
Ligands
CD, SO4
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProtein lgg-1protein11932% helix, 20% strandQ09490
C, DPeptide from autophagy-related protein 19protein40% helix, 50% strandP35193

Ligands and binding sites

  • CD · Cadmium ion · metal · 13 copies · chains A, B, D
  • SO4 · Sulfate ion · ion · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13890.720.8342empty

Interfaces

3 interfaces between chains.

  • A–B · 580 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 499 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 483 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 5AZF · Crystal structure of LGG-1 complexed with a WEEL peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • P35193 · AlphaFold monomer V2.0 prediction for autophagy-related protein 19 (P35193) · a predicted model of the same protein · chain C against A, TM-score 0.95
  • Q09490 · AlphaFold monomer V2.0 prediction for protein lgg-1 (Q09490) · a predicted model of the same protein · chain A against A, TM-score 0.93

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