Research workbench

Apo form of apolipoprotein N-acyltransferase (lnt)

Analyse Apo form of apolipoprotein N-acyltransferase (lnt) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q3A
Type: protein
Length: 492 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apolipoprotein N-acyltransferase
EC: 2.3.1.269
UniProt: P23930
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apolipoprotein N-acyltransferase (EC 2.3.1.269)	protein	492	49% helix, 15% strand	P23930

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A
OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 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	970	0.80	0.81	69	empty
2	190	0.59	0.82	30	empty
3	89	0.40	0.76	13	empty

Compared structures

6Q3A · Apo form of Apolipoprotein N-acyltransferase (Lnt) · 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 A against A, TM-score 0.99

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 6Q3A · PDBe 6Q3A · UniProt P23930

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