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Crystal structure of SeMet_Lpg0189

Analyse Crystal structure of SeMet_Lpg0189 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L6G
Type
protein
Length
528 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.98
Source
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 /…
Molecule
Uncharacterized protein Lpg0189
UniProt
Q5ZZ22
Pockets
5 · best druggability 0.67

Structure

x-ray diffraction · resolution 1.98 · 1 distinct chain · 28% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BUncharacterized protein Lpg0189protein26428% helix, 36% strandQ5ZZ22

Ligands and binding sites

  • GOL · Glycerol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14810.670.7950empty
22660.650.8234empty
3510.610.9322empty
41870.430.7333empty
5740.410.8015empty

Interfaces

1 interface between chains.

  • A–B · 1364 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified, 2 disulfide (engineered, disulfide).

Compared structures

  • 6L6G · Crystal structure of SEMET_LPG0189 · the same entry in another collection · chain A against A, TM-score 1.00

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