GL1X · GenesisL1 explorer

Research workbench

holo-form of polyphenol oxidase from Solanum lycopersicum

Analyse holo-form of polyphenol oxidase from Solanum lycopersicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HQI
Type
protein
Length
444 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.85
Source
Solanum lycopersicum
Molecule
Polyphenol oxidase A, chloroplastic
EC
1.10.3.1
Ligands
CU, O
Pockets
3 · best druggability 0.66

Structure

x-ray diffraction · resolution 1.85 · 1 distinct chain · 33% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolyphenol oxidase A, chloroplastic (EC 1.10.3.1)protein44433% helix, 20% strand—

Ligands and binding sites

  • CU · Copper (II) ion · metal · 2 copies · chains A
  • O · Oxygen atom · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12860.660.8249empty
2850.580.8719empty
3920.340.7419empty

Compared structures

  • 6HQI · Holo-form of polyphenol oxidase from solanum lycopersicum · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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