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Structure of xanthomonas campestris effector protein xopd bound to tomato sumo

Analyse Structure of xanthomonas campestris effector protein xopd bound to tomato sumo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5JP1
Type
protein
Length
276 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Xanthomonas outer protein D; Small ubiquitin-related modifier
UniProt
Q3BYJ5, Q9SMD1
Ligands
AYE, D1D
Pockets
3 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AXanthomonas outer protein Dprotein19940% helix, 15% strandQ3BYJ5
BSmall ubiquitin-related modifierprotein7718% helix, 36% strandQ9SMD1

Ligands and binding sites

  • AYE · prop-2-en-1-amine · ligand · chains A, B
  • D1D · (4S,5S)-1,2-dithiane-4,5-diol · ligand · chains A
  • MLI · Malonate ion · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11350.530.8123MLI
2810.430.8016empty
31360.430.7623empty

Interfaces

1 interface between chains.

  • A–B · 1226 Ų buried · 33 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 5JP1 · Structure of Xanthomonas campestris effector protein XopD bound to tomato SUMO · the same entry in another collection · chain A against A, TM-score 1.00

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