Chlorine in PDB 5nai: Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-D-Tryptophan (Compound 1)

The structure of Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-D-Tryptophan (Compound 1), PDB code: 5nai was solved by G.-B.Li, J.Brem, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	3.89 / 1.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.553, 67.555, 40.093, 90.00, 92.66, 90.00
R / Rfree (%)	13.1 / 14.1

The structure of Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-D-Tryptophan (Compound 1) also contains other interesting chemical elements:

Fluorine	(F)	2 atoms
Zinc	(Zn)	3 atoms

The binding sites of Chlorine atom in the Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-D-Tryptophan (Compound 1) (pdb code 5nai). 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 Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-D-Tryptophan (Compound 1), PDB code: 5nai:

Chlorine binding site 1 out of 1 in the Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-D-Tryptophan (Compound 1)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-D-Tryptophan (Compound 1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:20.5 occ:1.00 CL1 A:93W304 0.0 20.5 1.0 C07 A:93W304 1.8 20.6 1.0 N08 A:93W304 2.6 20.5 1.0 C05 A:93W304 2.8 21.0 1.0 C06 A:93W304 3.1 21.8 1.0 CG A:HIS240 3.4 12.8 1.0 NH2 A:ARG205 3.6 16.2 1.0 CD2 A:HIS240 3.6 14.4 1.0 C27 A:93W304 3.6 19.4 1.0 CB A:HIS240 3.7 13.6 1.0 ND1 A:HIS240 3.8 12.8 1.0 CD1 A:TYR67 3.8 16.3 1.0 C09 A:93W304 3.9 20.5 1.0 C28 A:93W304 4.0 19.2 1.0 C04 A:93W304 4.0 21.1 1.0 NE2 A:HIS240 4.1 15.6 1.0 CZ A:ARG205 4.1 17.9 1.0 CE1 A:HIS240 4.2 14.5 1.0 CG A:TYR67 4.3 14.8 1.0 O A:HOH605 4.3 29.9 1.0 CE1 A:TYR67 4.4 18.3 1.0 CB A:TYR67 4.4 15.4 1.0 C10 A:93W304 4.5 21.1 1.0 C01 A:93W304 4.5 22.7 1.0 C26 A:93W304 4.5 19.1 1.0 NH1 A:ARG205 4.6 19.8 1.0 O A:HOH573 4.6 28.8 0.5 O A:HOH604 4.7 32.8 1.0 O A:HOH573 4.7 21.4 0.5 NE A:ARG205 4.8 16.7 1.0 N14 A:93W304 5.0 20.0 1.0 O A:PRO68 5.0 13.2 1.0

G.B.Li, J.Brem, R.Lesniak, M.I.Abboud, C.T.Lohans, I.J.Clifton, S.Y.Yang, J.C.Jimenez-Castellanos, M.B.Avison, J.Spencer, M.A.Mcdonough, C.J.Schofield. Crystallographic Analyses of Isoquinoline Complexes Reveal A New Mode of Metallo-Beta-Lactamase Inhibition. Chem. Commun. (Camb.) V. 53 5806 2017.
ISSN: ESSN 1364-548X
PubMed: 28470248
DOI: 10.1039/C7CC02394D