Chlorine in PDB 8aq4: In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe

The structure of In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe, PDB code: 8aq4 was solved by C.-Y.Huang, D.Weichert, C.Boland, L.Smithers, V.Olieric, M.Wang, M.Caffrey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.13 / 2.62
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	160.111, 160.111, 90.934, 90, 90, 120
R / Rfree (%)	20.5 / 22.9

The binding sites of Chlorine atom in the In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe (pdb code 8aq4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe, PDB code: 8aq4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl621 b:65.0 occ:1.00 N A:GLY322 2.9 33.6 1.0 NE A:ARG289 3.3 75.9 1.0 CD A:ARG289 3.6 73.3 1.0 CA A:LYS321 3.7 25.0 1.0 C A:LYS321 3.7 19.8 1.0 CA A:GLY322 3.7 38.9 1.0 O A:GLY320 4.1 33.0 1.0 CG A:LYS321 4.4 48.4 1.0 CZ A:ARG289 4.5 77.9 1.0 CD A:PRO324 4.6 45.3 1.0 N A:ALA323 4.6 28.2 1.0 CB A:LYS321 4.7 30.4 1.0 CG A:ARG289 4.7 68.2 1.0 N A:LYS321 4.7 35.7 1.0 C A:GLY322 4.7 45.4 1.0 C A:GLY320 4.8 38.7 1.0 NH1 A:ARG289 4.8 81.5 1.0 O A:LYS321 4.8 33.3 1.0 CB A:ARG289 4.9 36.6 1.0

Chlorine binding site 2 out of 2 in the In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of In Surfo Structure of the Membrane Integral Lipoprotein N- Acyltransferase Lnt From E. Coli in Complex with Titc and Lyso-Pe within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl622 b:120.1 occ:1.00 NH2 A:ARG193 2.9 91.2 1.0 CD1 A:TRP121 3.1 131.5 1.0 N A:TRP121 3.5 85.5 1.0 NZ A:LYS189 3.7 77.8 1.0 CA A:THR120 3.7 75.7 1.0 CZ A:ARG193 3.9 111.2 1.0 NH1 A:ARG193 3.9 119.8 1.0 NE1 A:TRP121 4.0 132.4 1.0 CG A:TRP121 4.1 115.5 1.0 C A:THR120 4.1 77.2 1.0 CB A:THR120 4.3 71.1 1.0 O A:THR119 4.3 60.5 1.0 CB A:TRP121 4.4 97.3 1.0 CA A:TRP121 4.5 77.4 1.0 CE A:LYS189 4.8 93.4 1.0 CD2 A:LEU185 4.9 48.5 1.0 N A:THR120 4.9 66.9 1.0 CG2 A:THR120 4.9 73.0 1.0

L.Smithers, O.Degtjarik, D.Weichert, C.Y.Huang, C.Boland, K.Bowen, A.Oluwole, C.Lutomski, C.V.Robinson, E.M.Scanlan, M.Wang, V.Olieric, M.Shalev-Benami, M.Caffrey. Structure Snapshots Reveal the Mechanism of A Bacterial Membrane Lipoprotein N -Acyltransferase. Sci Adv V. 9 F5799 2023.
ISSN: ESSN 2375-2548
PubMed: 37390210
DOI: 10.1126/SCIADV.ADF5799