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Chlorine in PDB 7bdr: Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101)

Enzymatic activity of Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101)

All present enzymatic activity of Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101):
3.5.2.6;

Protein crystallography data

The structure of Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101), PDB code: 7bdr was solved by C.L.Tooke, P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.56 / 0.91
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.678, 45.671, 117.33, 90, 90, 90
R / Rfree (%) 11.4 / 12.6

Other elements in 7bdr:

The structure of Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101) also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101) (pdb code 7bdr). 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 Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101), PDB code: 7bdr:

Chlorine binding site 1 out of 1 in 7bdr

Go back to Chlorine Binding Sites List in 7bdr
Chlorine binding site 1 out of 1 in the Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Ctx-M-15 E166Q Mutant Crystallised in the Presence of Tazobactam (AAI101) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:9.6
occ:1.00
 H A:LYS269 2.5 10.8 1.0
HB3 A:GLN267 2.8 10.7 1.0
HB2 A:LYS269 2.8 13.3 1.0
HD2 A:PRO268 2.9 12.4 1.0
N A:LYS269 3.3 9.0 1.0
HG3 A:LYS269 3.4 16.6 1.0
CB A:LYS269 3.6 11.1 1.0
CD A:PRO268 3.7 10.4 1.0
CB A:GLN267 3.8 8.9 1.0
N A:PRO268 3.8 9.0 1.0
CA A:LYS269 3.9 9.5 1.0
HD2 A:LYS269 3.9 21.0 1.0
CG A:LYS269 4.0 13.8 1.0
HB2 A:PRO268 4.0 13.7 1.0
HB2 A:GLN267 4.1 10.7 1.0
C A:GLN267 4.2 8.3 1.0
HG2 A:PRO268 4.2 14.6 1.0
C A:PRO268 4.3 9.2 1.0
HA A:GLN267 4.3 10.4 1.0
CG A:PRO268 4.4 12.2 1.0
CA A:GLN267 4.4 8.7 1.0
C A:LYS269 4.4 9.1 1.0
HD3 A:PRO268 4.4 12.4 1.0
HB3 A:LYS269 4.4 13.3 1.0
CA A:PRO268 4.4 9.9 1.0
HG2 A:GLN267 4.4 11.6 1.0
CB A:PRO268 4.4 11.4 1.0
CD A:LYS269 4.5 17.5 1.0
H A:ALA270 4.6 9.7 1.0
CG A:GLN267 4.7 9.7 1.0
N A:ALA270 4.7 8.1 1.0
HA A:LYS269 4.8 11.4 1.0
HG2 A:LYS269 4.8 16.6 1.0
O A:GLN267 4.9 8.1 1.0
HE3 A:LYS269 5.0 24.3 1.0

Reference:

P.Hinchliffe, C.L.Tooke, C.R.Bethel, B.Wang, C.Arthur, K.J.Heesom, S.Shapiro, D.M.Schlatzer, K.M.Papp-Wallace, R.A.Bonomo, J.Spencer. Penicillanic Acid Sulfones Inactivate the Extended-Spectrum Beta-Lactamase Ctx-M-15 Through Formation of A Serine-Lysine Cross-Link: An Alternative Mechanism of Beta-Lactamase Inhibition. Mbio V. 13 79321 2022.
ISSN: ESSN 2150-7511
PubMed: 35612361
DOI: 10.1128/MBIO.01793-21
Page generated: Tue Apr 4 20:30:47 2023

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