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Crystal structure of AVRRXO1-ORF1:AVRRXO1-ORF2 with sulphate ions

Analyse Crystal structure of AVRRXO1-ORF1:AVRRXO1-ORF2 with sulphate ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4Z8T
Type
protein
Length
429 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
AVRRXO1-ORF1; AVRRXO1-ORF2
UniProt
Q6TKR8, Q6TKR9
Ligands
SO4
Pockets
4 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAVRRXO1-ORF1protein33152% helix, 13% strandQ6TKR8
BAVRRXO1-ORF2protein9867% helix, 1% strandQ6TKR9

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains A
  • GOL · Glycerol · additive · chains A
  • ACT · Acetate ion · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19350.850.86117SO4, GOL
22950.640.8031empty
3660.600.9122empty
41330.530.8125empty

Interfaces

1 interface between chains.

  • A–B · 1867 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 4Z8T · CRYSTAL STRUCTURE OF AvrRxo1-ORF1:AvrRxo1-ORF2 WITH SULPHATE IONS · the same entry in another collection · chain A against A, TM-score 1.00

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