Chlorine in PDB 5n55: Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2)

The structure of Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2), PDB code: 5n55 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)	50.68 / 1.99
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	66.219, 155.191, 267.733, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 25.3

The structure of Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2) also contains other interesting chemical elements:

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)-L-Tryptophan (Compound 2) (pdb code 5n55). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2), PDB code: 5n55:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2)


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)-L-Tryptophan (Compound 2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:33.7 occ:1.00 CL1 A:8NN502 0.0 33.7 1.0 C07 A:8NN502 1.8 25.8 1.0 N08 A:8NN502 2.7 29.4 1.0 C05 A:8NN502 2.7 20.4 1.0 C06 A:8NN502 2.9 37.2 1.0 CG A:ASN210 3.2 34.5 1.0 CE1 A:HIS116 3.3 25.2 1.0 CB A:ASN210 3.4 33.3 1.0 ND2 A:ASN210 3.5 36.3 1.0 OD1 A:ASN210 3.5 35.9 1.0 ND1 A:HIS116 3.6 29.4 1.0 O A:HOH652 3.6 25.1 1.0 C09 A:8NN502 3.9 27.7 1.0 O A:ASN210 3.9 30.7 1.0 C04 A:8NN502 4.0 20.9 1.0 NE2 A:HIS116 4.0 26.1 1.0 CE1 A:HIS179 4.1 23.6 1.0 O A:HOH649 4.1 74.0 1.0 C01 A:8NN502 4.3 42.2 1.0 NE2 A:HIS179 4.3 22.5 1.0 ZN A:ZN501 4.3 28.5 1.0 C10 A:8NN502 4.4 25.9 1.0 C A:ASN210 4.5 33.5 1.0 CG A:HIS116 4.5 22.9 1.0 CA A:ASN210 4.6 33.1 1.0 O A:HOH616 4.7 24.8 1.0 CD2 A:HIS116 4.7 26.3 1.0 N14 A:8NN502 5.0 28.7 1.0 O A:HOH621 5.0 36.3 1.0

Chlorine binding site 2 out of 3 in the Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:38.8 occ:1.00 CL1 B:8NN502 0.0 38.8 1.0 C07 B:8NN502 1.8 37.8 1.0 N08 B:8NN502 2.7 37.4 1.0 C05 B:8NN502 2.8 24.0 1.0 C06 B:8NN502 3.1 24.3 1.0 CE1 B:HIS116 3.2 24.2 1.0 ND2 B:ASN210 3.3 52.7 1.0 CG B:ASN210 3.3 37.5 1.0 ND1 B:HIS116 3.5 23.9 1.0 O B:HOH639 3.6 19.3 1.0 CB B:ASN210 3.6 30.0 1.0 O B:ASN210 3.7 33.0 1.0 OD1 B:ASN210 3.7 36.8 1.0 CE1 B:HIS179 3.9 24.1 1.0 C09 B:8NN502 3.9 28.2 1.0 NE2 B:HIS116 4.0 27.7 1.0 NE2 B:HIS179 4.1 32.5 1.0 ZN B:ZN501 4.1 21.1 1.0 C04 B:8NN502 4.1 27.0 1.0 CG B:HIS116 4.4 23.7 1.0 O B:HOH621 4.5 21.5 1.0 C B:ASN210 4.5 32.5 1.0 C01 B:8NN502 4.5 32.1 1.0 C10 B:8NN502 4.6 21.0 1.0 CD2 B:HIS116 4.6 25.1 1.0 CA B:ASN210 4.7 32.0 1.0 N14 B:8NN502 5.0 23.2 1.0

Chlorine binding site 3 out of 3 in the Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Mono-Zinc Vim-5 Metallo-Beta-Lactamase in Complex with (1-Chloro-4- Hydroxyisoquinoline-3-Carbonyl)-L-Tryptophan (Compound 2) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl502 b:51.5 occ:1.00 CL1 C:8NN502 0.0 51.5 1.0 C07 C:8NN502 1.8 42.7 1.0 N08 C:8NN502 2.6 37.6 1.0 C05 C:8NN502 2.8 38.3 1.0 C06 C:8NN502 3.0 34.8 1.0 CG C:ASN210 3.2 49.4 1.0 ND2 C:ASN210 3.3 59.5 1.0 CE1 C:HIS116 3.3 32.0 1.0 OD1 C:ASN210 3.5 50.1 1.0 O C:HOH627 3.5 22.5 1.0 CB C:ASN210 3.5 45.6 1.0 ND1 C:HIS116 3.7 30.9 1.0 O C:ASN210 3.8 43.0 1.0 NE2 C:HIS116 3.8 32.7 1.0 C09 C:8NN502 3.9 31.2 1.0 C04 C:8NN502 4.0 29.5 1.0 CE1 C:HIS179 4.3 29.5 1.0 ZN C:ZN501 4.4 30.0 1.0 C01 C:8NN502 4.4 33.4 1.0 C C:ASN210 4.4 42.3 1.0 CG C:HIS116 4.4 31.0 1.0 CD2 C:HIS116 4.4 32.7 1.0 C10 C:8NN502 4.5 29.5 1.0 CA C:ASN210 4.6 46.0 1.0 NE2 C:HIS179 4.6 28.8 1.0 OD2 C:ASP213 4.7 53.7 1.0 O C:HOH605 4.9 41.3 1.0 N14 C:8NN502 4.9 32.4 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