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Cryo-EM structure of the multiple peptide resistance factor (mprf) loaded with one lysyl-phosphatidylglycerol molecule

Analyse Cryo-EM structure of the multiple peptide resistance factor (mprf) loaded with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LVF
Type
protein
Length
1,586 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Low pH-inducible protein lpia
UniProt
L0LM43
Ligands
EV9, LHG, PGT
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 56% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, ALow pH-inducible protein lpiaprotein79356% helix, 8% strandL0LM43

Ligands and binding sites

  • EV9 · [(2~{R})-3-[[(2~{S})-3-[(2~{S})-2,6-bis(azanyl) hexanoyl]oxy-2-oxidanyl-propoxy]-oxidanyl-phosphoryl]oxy-2-hexadecanoyloxy-propyl] hexadecanoate · ligand · 2 copies · chains B, A
  • LHG · 1,2-dipalmitoyl-phosphatidyl-glycerole · ligand · 2 copies · chains B, A
  • PGT · (1S)-2-{[{[(2R)-2,3-dihydroxypropyl]oxy}(hydroxy) phosphoryl]oxy}-1-[(palmitoyloxy)methyl]ethyl stearate · ligand · 2 copies · chains B, A

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110540.860.8692LHG, PGT
210940.850.86111EV9
311070.850.86113EV9
47660.810.8475empty
58480.810.8377empty

Interfaces

1 interface between chains.

  • B–A · 732 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6LVF · Cryo-EM structure of the multiple peptide resistance factor (MprF) loaded with one… · the same entry in another collection · chain B against B, TM-score 1.00

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