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Structure of the lipoprotein transporter LolA from Porphyromonas gingivalis

Analyse Structure of the lipoprotein transporter LolA from Porphyromonas gingivalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8CGM
Type
protein
Length
380 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.7
Source
Porphyromonas gingivalis ATCC 33277
Molecule
Outer membrane lipoprotein carrier protein LolA
UniProt
Q7MUA1
Pockets
6 · best druggability 0.62

Structure

x-ray diffraction · resolution 1.7 · 1 distinct chain · 17% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BOuter membrane lipoprotein carrier protein LolAprotein19017% helix, 48% strandQ7MUA1

Ligands and binding sites

  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
  • FMT · Formic acid · additive · 2 copies · chains B
  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14470.620.7652empty
22570.590.7835MES
32410.570.7839MES
42530.500.7538empty
5590.380.7913empty

Interfaces

1 interface between chains.

  • A–B · 740 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

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