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Structure of the dirigent protein DRR206

Analyse Structure of the dirigent protein DRR206 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4REV
Type
protein
Length
255 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Disease resistance response protein 206
UniProt
P13240
Ligands
DMI, CL
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 64% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADisease resistance response protein 206protein1280% helix, 64% strandP13240
BDisease resistance response protein 206protein1270% helix, 63% strandP13240

Ligands and binding sites

  • DMI · 2,3-dimethylimidazolium ion · ligand · chains B
  • CL · Chloride ion · ion · 2 copies · chains B
  • GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12570.620.8024empty
22500.580.7823empty
32020.550.7828empty

Interfaces

1 interface between chains.

  • A–B · 392 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4REV · Structure of the dirigent protein DRR206 · the same entry in another collection · chain A against A, TM-score 1.00
  • P13240 · AlphaFold monomer V2.0 prediction for disease resistance response protein 206 (P13240) · a predicted model of the same protein · chain B against A, TM-score 0.84

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