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Crystal structure of the fatty ACID/PHOSPHOLIPID synthesis protein plsx from enterococcus faecalis V583

Analyse Crystal structure of the fatty ACID/PHOSPHOLIPID synthesis protein plsx from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1U7N
Type
protein
Length
636 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fatty ACID/PHOSPHOLIPID synthesis protein plsx
UniProt
Q82ZE8
Pockets
7 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFatty ACID/PHOSPHOLIPID synthesis protein plsxprotein31848% helix, 17% strandQ82ZE8
BFatty ACID/PHOSPHOLIPID synthesis protein plsxprotein31848% helix, 17% strandQ82ZE8

Ligands and binding sites

  • EOH · Ethanol · additive · 4 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16820.680.7678EOH
24680.640.7751empty
31850.590.8122EOH
4570.350.7815empty
5720.330.7515empty

Interfaces

1 interface between chains.

  • A–B · 1826 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 26 modified (engineered).

Compared structures

  • 1U7N · Crystal Structure of the fatty acid/phospholipid synthesis protein PlsX from Enterococcus… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q82ZE8 · AlphaFold monomer V2.0 prediction for phosphate acyltransferase (Q82ZE8) · a predicted model of the same protein · chain B against A, TM-score 0.98

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