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Crystal structure of the tir domain from the grapevine disease resistance protein RUN1 without the ae interface

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

PDB: 7RTS
Type: protein
Length: 163 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Disease resistance protein RUN1
EC: 3.2.2.6, 3.2.2.-
UniProt: V9M398
Ligands: SO4
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Disease resistance protein RUN1 (EC 3.2.2.6, 3.2.2.-)	protein	163	52% helix, 17% strand	V9M398

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.30	0.75	15	SO4

Compared structures

7RTS · Crystal structure of the TIR domain from the grapevine disease resistance protein RUN1… · the same entry in another collection · chain A against A, TM-score 1.00
V9M398 · AlphaFold monomer V2.0 prediction for disease resistance protein RUN1 (V9M398) · a predicted model of the same protein · chain A against A, TM-score 0.90

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt V9M398
Elsewhere: RCSB PDB 7RTS · PDBe 7RTS · UniProt V9M398

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