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Zinc in PDB 5evk: Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319

Enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319, PDB code: 5evk was solved by P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.87 / 1.63
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 104.980, 104.980, 98.465, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 18.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319 (pdb code 5evk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319, PDB code: 5evk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5evk

Go back to Zinc Binding Sites List in 5evk
Zinc binding site 1 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:18.7
occ:1.00
OD2 A:ASP120 2.0 17.8 1.0
NE2 A:HIS121 2.0 17.1 1.0
NE2 A:HIS263 2.1 16.6 1.0
S01 A:3C7401 2.2 23.5 1.0
CG A:ASP120 2.7 19.6 1.0
CE1 A:HIS121 2.8 17.1 1.0
OD1 A:ASP120 2.9 16.3 1.0
CD2 A:HIS121 3.0 17.0 1.0
CE1 A:HIS263 3.0 18.7 1.0
CD2 A:HIS263 3.1 16.8 1.0
C02 A:3C7401 3.3 42.3 1.0
C03 A:3C7401 3.6 54.9 1.0
ZN A:ZN404 3.9 19.0 1.0
ND1 A:HIS121 3.9 17.2 1.0
CG A:HIS121 4.0 15.9 1.0
ND1 A:HIS263 4.1 17.8 1.0
CB A:ASP120 4.1 16.3 1.0
CG A:HIS263 4.2 17.6 1.0
NE2 A:HIS116 4.3 15.2 1.0
CE1 A:HIS116 4.3 13.5 1.0
C08 A:3C7401 4.4 47.2 1.0
N07 A:3C7401 4.4 53.0 1.0
O A:HOH501 4.5 53.4 1.0
OG A:SER221 4.9 22.1 1.0
CH2 A:TRP39 4.9 24.3 1.0
CZ3 A:TRP39 5.0 21.2 1.0
S04 A:3C7401 5.0 60.6 1.0
CD2 A:LEU69 5.0 18.9 1.0
C A:ASP120 5.0 16.2 1.0

Zinc binding site 2 out of 2 in 5evk

Go back to Zinc Binding Sites List in 5evk
Zinc binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Metallo-Beta-Lactamase L1 in Complex with the Bisthiazolidine Inhibitor L-CS319 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn404

b:19.0
occ:1.00
ND1 A:HIS118 2.0 17.8 1.0
NE2 A:HIS116 2.1 15.2 1.0
NE2 A:HIS196 2.1 18.4 1.0
S01 A:3C7401 2.3 23.5 1.0
CE1 A:HIS118 2.9 17.1 1.0
C02 A:3C7401 3.0 42.3 1.0
CD2 A:HIS196 3.0 17.7 1.0
CD2 A:HIS116 3.0 14.4 1.0
CE1 A:HIS116 3.0 13.5 1.0
CG A:HIS118 3.1 15.7 1.0
CE1 A:HIS196 3.2 17.4 1.0
CB A:HIS118 3.5 16.6 1.0
ZN A:ZN403 3.9 18.7 1.0
NE2 A:HIS118 4.0 16.9 1.0
ND1 A:HIS116 4.1 16.2 1.0
CG A:HIS116 4.1 15.3 1.0
CD2 A:HIS118 4.1 16.3 1.0
CG A:HIS196 4.2 16.8 1.0
CD2 A:HIS121 4.3 17.0 1.0
ND1 A:HIS196 4.3 18.0 1.0
OD1 A:ASP120 4.3 16.3 1.0
NE2 A:HIS121 4.4 17.1 1.0
C03 A:3C7401 4.4 54.9 1.0
CA A:HIS118 4.9 16.8 1.0

Reference:

P.Hinchliffe, M.M.Gonzalez, M.F.Mojica, J.M.Gonzalez, V.Castillo, C.Saiz, M.Kosmopoulou, C.L.Tooke, L.I.Llarrull, G.Mahler, R.A.Bonomo, A.J.Vila, J.Spencer. Cross-Class Metallo-Beta-Lactamase Inhibition By Bisthiazolidines Reveals Multiple Binding Modes. Proc.Natl.Acad.Sci.Usa V. 113 E3745 2016.
ISSN: ESSN 1091-6490
PubMed: 27303030
DOI: 10.1073/PNAS.1601368113
Page generated: Sun Oct 27 15:35:19 2024

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