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Crystal structure of the tir domain from the arabidopsis thaliana disease resistance protein RPP1

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

PDB
5TEB
Type
protein
Length
1,315 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Recognition of peronospora parasitica 1
UniProt
D9IW02
Pockets
20 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 54% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FRecognition of peronospora parasitica 1protein16659% helix, 14% strandD9IW02
GRecognition of peronospora parasitica 1protein15951% helix, 13% strandD9IW02
HRecognition of peronospora parasitica 1protein16051% helix, 16% strandD9IW02

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12820.680.8326empty
25450.680.7841empty
33170.670.8139empty
41930.660.8532empty
54290.640.7839empty

Interfaces

11 interfaces between chains.

  • A–B · 666 Ų buried · 7 hydrogen bonds · protein-protein
  • D–E · 615 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 468 Ų buried · 3 hydrogen bonds · protein-protein
  • E–H · 461 Ų buried · 5 hydrogen bonds · protein-protein
  • D–G · 454 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5TEB · Crystal Structure of the TIR domain from the Arabidopsis Thaliana disease resistance… · the same entry in another collection · chain A against A, TM-score 1.00

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