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Crystal structure of nn domain of resistance protein

Analyse Crystal structure of nn domain of resistance protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3WRV
Type
protein
Length
365 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tm-1 protein
UniProt
A7M6E7
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATm-1 proteinprotein19247% helix, 17% strandA7M6E7
BTm-1 proteinprotein17345% helix, 18% strandA7M6E7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1760.530.8516empty
2600.490.8517empty

Interfaces

1 interface between chains.

  • A–B · 1225 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 3WRV · Crystal structure of NN domain of resistance protein · the same entry in another collection · chain A against A, TM-score 1.00
  • A7M6E7 · AlphaFold monomer V2.0 prediction for tomv resistance protein tm-1(GCR237) (A7M6E7) · a predicted model of the same protein · chain A against A, TM-score 0.96

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