Chlorine in PDB 5vrh: Apolipoprotein N-Acyltransferase C387S Active Site Mutant

The structure of Apolipoprotein N-Acyltransferase C387S Active Site Mutant, PDB code: 5vrh was solved by J.M.Murray, C.L.Noland, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.04 / 2.14
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.671, 72.586, 75.610, 90.00, 101.73, 90.00
R / Rfree (%)	20.7 / 25

The structure of Apolipoprotein N-Acyltransferase C387S Active Site Mutant also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the Apolipoprotein N-Acyltransferase C387S Active Site Mutant (pdb code 5vrh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Apolipoprotein N-Acyltransferase C387S Active Site Mutant, PDB code: 5vrh:

Chlorine binding site 1 out of 1 in the Apolipoprotein N-Acyltransferase C387S Active Site Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Apolipoprotein N-Acyltransferase C387S Active Site Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl606 b:32.9 occ:0.90 NZ A:LYS236 3.0 29.1 1.0 OD1 A:ASN412 3.1 30.4 1.0 NE1 A:TRP415 3.1 33.6 1.0 NE1 A:TRP237 3.3 34.9 1.0 NE2 A:GLN233 3.7 28.3 1.0 CD A:LYS236 3.8 29.7 1.0 CE A:LYS236 4.0 28.8 1.0 CE2 A:TRP415 4.0 36.4 1.0 CG A:ASN412 4.0 26.1 1.0 CE2 A:TRP237 4.0 36.6 1.0 CZ2 A:TRP237 4.1 37.1 1.0 CD1 A:TRP415 4.1 32.1 1.0 OG A:SER268 4.1 25.7 0.6 CZ2 A:TRP415 4.2 38.0 1.0 C22 A:OLC607 4.3 54.0 0.9 O23 A:OLC607 4.3 54.1 0.9 CB A:ASN412 4.3 25.2 1.0 OE1 A:GLN233 4.3 31.4 1.0 CD1 A:TRP237 4.4 36.5 1.0 CD A:GLN233 4.5 29.6 1.0 O23 A:OLC608 4.7 51.4 1.0 O25 A:OLC607 4.9 52.8 0.9 C24 A:OLC607 5.0 53.6 0.9

C.L.Noland, M.D.Kattke, J.Diao, S.L.Gloor, H.Pantua, M.Reichelt, A.K.Katakam, D.Yan, J.Kang, I.Zilberleyb, M.Xu, S.B.Kapadia, J.M.Murray. Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase. Proc. Natl. Acad. Sci. V. 114 E6044 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28698362
DOI: 10.1073/PNAS.1707813114