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In meso structure of apolipoprotein N-acyltransferase, Lnt, from Escherichia coli in 7.10 monoacylglycerol

Analyse In meso structure of apolipoprotein N-acyltransferase, Lnt, from Escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8RQR
Type: protein
Length: 511 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.19
Source: Escherichia coli
Molecule: Apolipoprotein N-acyltransferase
EC: 2.3.1.269
UniProt: P23930
Ligands: A1H2K
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · resolution 2.19 · 1 distinct chain · 53% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apolipoprotein N-acyltransferase (EC 2.3.1.269)	protein	511	53% helix, 16% strand	P23930

Ligands and binding sites

A1H2K · 7.10 monoacylglycerol (S-form) · ligand · 8 copies · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	850	0.76	0.79	68	A1H2K
2	196	0.62	0.83	29	empty
3	65	0.33	0.75	13	empty

Compared structures

P23930 · AlphaFold monomer V2.0 prediction for apolipoprotein N-acyltransferase (P23930) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P23930
Elsewhere: RCSB PDB 8RQR · PDBe 8RQR · UniProt P23930

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