MolNFT v1 · #172754 · protein

In meso structure of apolipoprotein N-acyltransferase, lnt, from escherichia COLI in 9.8 monoacylglycerol

7ACI: “In meso structure of apolipoprotein N-acyltransferase, lnt, from escherichia COLI in 9.8 monoacylglycerol”. X-ray diffraction, 1 ligand (LH9), 3 pockets (best druggability 0.75). MolNFT v1 #172754 on GenesisL1: 3D structure, binding…

PDB: 7ACI
Type: protein
Length: 505 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: A0A037YBN4
Ligands: LH9
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apolipoprotein N-acyltransferase (EC 2.3.1.269)	protein	505	51% helix, 16% strand	A0A037YBN4

Ligands and binding sites

LH9 · [(2~{S})-2,3-bis(oxidanyl)propyl] heptadec-9-enoate · ligand · 6 copies · chains A
GOL · Glycerol · additive · 6 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	598	0.75	0.81	59	LH9
2	178	0.59	0.82	24	empty
3	61	0.34	0.76	11	empty

Compared structures

7ACI · In meso structure of apolipoprotein N-acyltransferase, Lnt, from Escherichia coli in 9.8… · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A037YBN4
Elsewhere: RCSB PDB 7ACI · PDBe 7ACI · UniProt A0A037YBN4

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