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Structural insight into the biological functions of arabidopsis thaliana ACHT1

Analyse Structural insight into the biological functions of arabidopsis thaliana ACHT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LYW
Type
protein
Length
239 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thioredoxin-like 2-1, chloroplastic
UniProt
Q8LEK4
Ligands
SO4
Pockets
1 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThioredoxin-like 2-1, chloroplasticprotein12142% helix, 26% strandQ8LEK4
BThioredoxin-like 2-1, chloroplasticprotein11843% helix, 25% strandQ8LEK4

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A, B
  • GOL · Glycerol · additive · 3 copies · chains A, 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11610.430.7425empty

Interfaces

1 interface between chains.

  • A–B · 517 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 6LYW · Structural insight into the biological functions of Arabidopsis thaliana ACHT1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8LEK4 · AlphaFold monomer V2.0 prediction for thioredoxin-like 2-1, chloroplastic (Q8LEK4) · a predicted model of the same protein · chain B against A, TM-score 1.00

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