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Crystal structure of pathogenesis-related protein llpr-10.2A from yellow lupine

Analyse Crystal structure of pathogenesis-related protein llpr-10.2A from yellow lupine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XDF
Type
protein
Length
314 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
PR10.2A
UniProt
Q9LLQ3
Ligands
NA
Pockets
2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPR10.2Aprotein15728% helix, 44% strandQ9LLQ3

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12500.550.7727empty
21180.380.7519empty

Interfaces

1 interface between chains.

  • A–B · 506 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1XDF · Crystal structure of pathogenesis-related protein LlPR-10.2A from yellow lupine · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9LLQ3 · AlphaFold monomer V2.0 prediction for class 10 plant pathogenesis- related protein 2A… · a predicted model of the same protein · chain A against A, TM-score 0.85

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