GL1X · GenesisL1 explorer

Research workbench

Crystal structure of WHY3 from arabidopsis thaliana

Analyse Crystal structure of WHY3 from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4KOQ
Type
protein
Length
169 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Single-stranded DNA-binding protein WHY3, chloroplastic
UniProt
Q66GR6
Ligands
PO4
Pockets
1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASingle-stranded DNA-binding protein WHY3, chloroplasticprotein16922% helix, 43% strandQ66GR6

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.350.7812empty

Compared structures

  • 4KOQ · Crystal Structure of WHY3 from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
  • Q66GR6 · AlphaFold monomer V2.0 prediction for single-stranded DNA-binding protein WHY3… · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.