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Crystal structure of LPG1832, a virk family protein from legionella pneumophila

Analyse Crystal structure of LPG1832, a virk family protein from legionella pneumophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XTA
Type
protein
Length
480 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Virk protein
UniProt
A0A128ZU06
Ligands
SO4
Pockets
7 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DVirk proteinprotein12013% helix, 53% strandA0A128ZU06

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B, C, D
  • GOL · Glycerol · additive · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16860.850.8945SO4, GOL
24390.750.8439empty
34010.740.8438empty
43830.740.8439empty
54260.730.8340empty

Interfaces

6 interfaces between chains.

  • A–D · 920 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 916 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 896 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 896 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 26 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified, 3 disulfide (engineered, disulfide).

Compared structures

  • 5XTA · Crystal structure of lpg1832, a VirK family protein from Legionella pneumophila · the same entry in another collection · chain A against A, TM-score 1.00

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