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Crystal structure of in planta processed AVRRPS4 in complex with the wrky domain of RRS1

Analyse Crystal structure of in planta processed AVRRPS4 in complex with the wrky… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P8K
Type: protein
Length: 126 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Disease resistance protein RRS1; Avirulence PROTEIN,AVIRULENCE protein
UniProt: C4B7M5, Q52432
Ligands: ZN

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Disease resistance protein RRS1	protein	64	0% helix, 39% strand	C4B7M5
A	Avirulence PROTEIN,AVIRULENCE protein	protein	62	92% helix, 0% strand	Q52432

Ligands and binding sites

ZN · Zinc ion · metal · chains B

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

Interfaces

1 interface between chains.

B–A · 636 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

7P8K · Crystal structure of in planta processed AvrRps4 in complex with the WRKY domain of RRS1 · the same entry in another collection · chain B against B, TM-score 1.00
C4B7M5 · AlphaFold monomer V2.0 prediction for disease resistance protein RRS1 (C4B7M5) · a predicted model of the same protein · chain B against A, TM-score 0.86

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 C4B7M5
Every structure of UniProt Q52432
Elsewhere: RCSB PDB 7P8K · PDBe 7P8K · UniProt C4B7M5 · UniProt Q52432

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