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Crystal structure of yellow lupine llpr-10.1A protein in ligand-free form

Analyse Crystal structure of yellow lupine llpr-10.1A protein in ligand-free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4Y31
Type
protein
Length
150 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein LLR18A
UniProt
P52778
Pockets
1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein LLR18Aprotein15025% helix, 45% strandP52778

Ligands and binding sites

  • ACT · Acetate ion · additive · chains A

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
13440.660.8052empty

Compared structures

  • 4Y31 · Crystal structure of yellow lupine LlPR-10.1A protein in ligand-free form · the same entry in another collection · chain A against A, TM-score 1.00
  • P52778 · AlphaFold monomer V2.0 prediction for protein LLR18A (P52778) · a predicted model of the same protein · chain A against A, TM-score 0.92

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