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Chlorine in PDB 5vrg: Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase

Protein crystallography data

The structure of Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase, PDB code: 5vrg 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) 43.07 / 2.52
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 87.764, 158.026, 44.763, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 27.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase (pdb code 5vrg). 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 Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase, PDB code: 5vrg:

Chlorine binding site 1 out of 1 in 5vrg

Go back to Chlorine Binding Sites List in 5vrg
Chlorine binding site 1 out of 1 in the Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Insights Into Lipoprotein N-Acylation By Escherichia Coli Apolipoprotein N-Acyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl608

b:49.8
occ:0.76
CE A:LYS236 3.0 70.1 1.0
ND2 A:ASN412 3.1 35.7 1.0
NE1 A:TRP237 3.3 65.5 1.0
O25 A:OLC601 3.8 59.2 1.0
CZ2 A:TRP237 3.9 64.2 1.0
NE1 A:TRP415 3.9 62.7 1.0
CE2 A:TRP237 3.9 65.6 1.0
NZ A:LYS236 3.9 69.1 1.0
NE2 A:GLN233 3.9 65.3 1.0
CZ2 A:TRP415 4.0 65.9 1.0
CD A:LYS236 4.1 71.6 1.0
CG A:ASN412 4.1 33.7 1.0
CB A:ASN412 4.1 31.0 1.0
CG A:LYS236 4.2 72.8 1.0
CE2 A:TRP415 4.3 64.7 1.0
CD1 A:TRP237 4.4 67.9 1.0
C22 A:OLC601 4.4 60.0 1.0
OE1 A:GLN233 4.5 63.5 1.0
CD A:GLN233 4.6 64.6 1.0
C24 A:OLC601 4.8 59.6 1.0
CB A:SER268 4.8 31.9 1.0
O A:GLU267 5.0 25.3 1.0

Reference:

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
Page generated: Sat Jul 12 10:00:45 2025

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