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Crystal structure of protein LPP20 (HP1456) from helicobacter pylori

Analyse Crystal structure of protein LPP20 (HP1456) from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OK8
Type
protein
Length
457 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LPP20 lipoprotein
UniProt
P0A0V1
Ligands
CA
Pockets
6 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, DLPP20 lipoproteinprotein11455% helix, 22% strandP0A0V1
BLPP20 lipoproteinprotein11555% helix, 22% strandP0A0V1

Ligands and binding sites

  • CA · Calcium ion · metal · chains B
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18230.740.7981EPE, CA
2590.360.7914empty
3770.350.7618empty
4880.340.7414empty
5560.280.7310empty

Interfaces

4 interfaces between chains.

  • C–D · 527 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 312 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 200 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 58 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5OK8 · Crystal structure of protein Lpp20 (HP1456) from Helicobacter pylori · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A0V1 · AlphaFold monomer V2.0 prediction for LPP20 lipoprotein (P0A0V1) · a predicted model of the same protein · chain B against A, TM-score 0.97

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