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Sodium in PDB 5ev8: Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319

Enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319, PDB code: 5ev8 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) 37.24 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.560, 77.713, 261.638, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 22

Other elements in 5ev8:

The structure of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319 also contains other interesting chemical elements:

Zinc (Zn) 8 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319 (pdb code 5ev8). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319, PDB code: 5ev8:

Sodium binding site 1 out of 1 in 5ev8

Go back to Sodium Binding Sites List in 5ev8
Sodium binding site 1 out of 1 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 in Complex with the Bisthiazolidine Inhibitor D-CS319 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na306

b:53.3
occ:1.00
 O C:HOH438 3.7 40.5 1.0
OE2 C:GLU150 3.9 66.6 1.0
O C:LEU39 4.2 42.3 1.0
CG1 C:VAL38 4.3 30.3 1.0
CG C:ARG151 4.4 39.4 1.0
NH1 C:ARG151 4.4 63.3 1.0
CZ C:ARG151 4.5 67.0 1.0
CB C:GLU150 4.6 45.5 1.0
O C:GLY15 4.7 41.1 1.0
O C:GLU14 4.7 47.7 1.0
NH2 C:ARG151 4.8 65.6 1.0
CG2 C:VAL16 4.8 36.7 1.0
CG2 C:VAL40 4.9 41.8 1.0
CD C:GLU150 4.9 60.9 1.0
NE C:ARG151 4.9 57.8 1.0
O C:HOH442 5.0 58.2 1.0
O C:LYS129 5.0 38.4 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: Mon Oct 7 20:52:53 2024

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