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Chlorine in PDB 7qq5: Structure of Ctx-M-15 K73A Mutant Crystallised in the Presence of Enmetazobactam (AAI101)

Enzymatic activity of Structure of Ctx-M-15 K73A Mutant Crystallised in the Presence of Enmetazobactam (AAI101)

All present enzymatic activity of Structure of Ctx-M-15 K73A Mutant Crystallised in the Presence of Enmetazobactam (AAI101):
3.5.2.6;

Protein crystallography data

The structure of Structure of Ctx-M-15 K73A Mutant Crystallised in the Presence of Enmetazobactam (AAI101), PDB code: 7qq5 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) 42.39 / 0.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.776, 45.465, 117.235, 90, 90, 90
R / Rfree (%) 14.4 / 16.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Ctx-M-15 K73A Mutant Crystallised in the Presence of Enmetazobactam (AAI101) (pdb code 7qq5). 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 K73A Mutant Crystallised in the Presence of Enmetazobactam (AAI101), PDB code: 7qq5:

Chlorine binding site 1 out of 1 in 7qq5

Go back to Chlorine Binding Sites List in 7qq5
Chlorine binding site 1 out of 1 in the Structure of Ctx-M-15 K73A Mutant Crystallised in the Presence of Enmetazobactam (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 K73A Mutant Crystallised in the Presence of Enmetazobactam (AAI101) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:10.9
occ:1.00
 H A:ALA227 2.4 11.2 1.0
HA A:PRO226 3.0 11.1 1.0
O A:HOH729 3.1 35.1 1.0
O A:HOH631 3.2 14.1 1.0
N A:ALA227 3.3 9.3 1.0
HB3 A:PRO226 3.5 11.8 1.0
HB3 A:ALA227 3.5 15.3 1.0
HB2 A:ALA227 3.7 15.3 1.0
CA A:PRO226 3.7 9.2 1.0
CB A:ALA227 4.0 12.8 1.0
C A:PRO226 4.0 8.8 1.0
CB A:PRO226 4.1 9.9 1.0
CA A:ALA227 4.2 11.4 1.0
H A:SER228 4.5 13.9 1.0
HB2 A:PRO226 4.7 11.8 1.0
O A:HOH644 4.7 30.8 1.0
O A:HOH685 4.7 39.2 1.0
HG3 A:PRO226 4.8 12.0 1.0
HA A:ALA227 4.9 13.7 1.0
HB1 A:ALA227 4.9 15.3 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: Sun Jul 13 06:26:10 2025

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