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AlphaFold monomer V2.0 prediction for single-stranded DNA-binding protein WHY1, chloroplastic (Q9M9S3)

Analyse AlphaFold monomer V2.0 prediction for single-stranded DNA-binding protein WHY1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q9M9S3
Type
protein
Length
263 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
Molecule
Single-stranded DNA-binding protein WHY1, chloroplastic
UniProt
Q9M9S3
Pockets
1 · best druggability 0.41

Structure

1 distinct chain · 17% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASingle-stranded DNA-binding protein WHY1, chloroplasticprotein26317% helix, 28% strandQ9M9S3

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11180.410.7621empty

Compared structures

  • 4KOO · Crystal Structure of WHY1 from Arabidopsis thaliana · an experimental structure of the same protein · chain A against D, TM-score 0.64
  • 4KOO · Crystal structure of WHY1 from arabidopsis thaliana · an experimental structure of the same protein · chain A against D, TM-score 0.64

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