GL1X · GenesisL1 explorer

Research workbench

Crystal structure of hyaloperonospora arabidopsidis ATR1 effector domain

Analyse Crystal structure of hyaloperonospora arabidopsidis ATR1 effector domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3RMR
Type
protein
Length
702 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Avirulence protein
UniProt
Q4VKJ6
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 73% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAvirulence proteinprotein23673% helix, 0% strandQ4VKJ6
BAvirulence proteinprotein23173% helix, 0% strandQ4VKJ6
CAvirulence proteinprotein23573% helix, 0% strandQ4VKJ6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111020.780.8084empty
22970.550.7629empty
3670.400.8019empty
4540.380.8018empty
5940.380.7623empty

Interfaces

3 interfaces between chains.

  • A–B · 1483 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 1257 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 299 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

  • 3RMR · Crystal structure of Hyaloperonospora arabidopsidis ATR1 effector domain · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.