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Structure of the membrane integral lipoprotein N-acyltransferase lnt from E. COLI

Analyse Structure of the membrane integral lipoprotein N-acyltransferase lnt from E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5N6H
Type
protein
Length
1,001 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Apolipoprotein N-acyltransferase
EC
2.3.1.-
UniProt
P23930
Pockets
9 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AApolipoprotein N-acyltransferase (EC 2.3.1.-)protein50350% helix, 16% strandP23930
BApolipoprotein N-acyltransferase (EC 2.3.1.-)protein49851% helix, 17% strandP23930

Ligands and binding sites

  • OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 18 copies · chains A, B
  • GOL · Glycerol · additive · 13 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17630.760.8063empty
27700.750.7962empty
32050.610.8227empty
42160.610.8226empty
5830.370.7515empty

Interfaces

1 interface between chains.

  • A–B · 74 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

  • 5N6H · Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
  • P23930 · AlphaFold monomer V2.0 prediction for apolipoprotein N-acyltransferase (P23930) · a predicted model of the same protein · chain B against A, TM-score 0.99

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