Fluorine in PDB 7s0v: The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase

All present enzymatic activity of The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase:
3.5.2.6;

The structure of The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase, PDB code: 7s0v was solved by M.T.Kemp, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.53 / 1.95
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	41.62, 41.62, 231.162, 90, 90, 120
R / Rfree (%)	18.9 / 25.9

The binding sites of Fluorine atom in the The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase (pdb code 7s0v). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase, PDB code: 7s0v:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:23.4 occ:0.91 F07 A:J1X301 0.0 23.4 0.9 C06 A:J1X301 1.4 15.3 0.9 F08 A:J1X301 2.2 15.0 0.9 F09 A:J1X301 2.2 20.2 0.9 C05 A:J1X301 2.3 16.5 0.9 HG23 A:THR171 2.7 12.0 1.0 HA A:THR171 3.0 14.2 1.0 C04 A:J1X301 3.0 10.0 0.9 HG22 A:THR171 3.0 12.0 1.0 HB2 A:ASN170 3.0 11.4 1.0 C10 A:J1X301 3.1 10.2 0.9 N A:THR171 3.2 8.1 1.0 HA A:THR168 3.2 9.6 1.0 O A:PRO167 3.2 10.2 1.0 C A:ASN170 3.3 6.8 1.0 CG2 A:THR171 3.3 10.0 1.0 H A:ASN170 3.4 8.4 1.0 H A:THR171 3.4 9.8 1.0 CA A:THR171 3.5 11.8 1.0 O A:ASN170 3.6 5.5 1.0 CB A:ASN170 3.8 9.5 1.0 CA A:ASN170 3.8 5.0 1.0 N A:ASN170 3.9 7.0 1.0 CB A:THR171 4.0 5.9 1.0 O A:HOH614 4.0 27.2 1.0 CA A:THR168 4.0 8.0 1.0 HG21 A:THR171 4.1 12.0 1.0 O A:THR168 4.1 6.5 1.0 C A:PRO167 4.1 7.5 1.0 C03 A:J1X301 4.2 13.9 0.9 HB3 A:ASN170 4.2 11.4 1.0 C A:THR168 4.2 8.4 1.0 C11 A:J1X301 4.3 18.2 0.9 HD22 A:ASN170 4.4 17.5 1.0 HB2 A:PRO167 4.4 10.5 1.0 HB2 A:ASP240 4.5 15.9 1.0 N A:THR168 4.6 8.5 1.0 HB A:THR171 4.6 7.1 1.0 O A:HOH410 4.7 28.6 1.0 C17 A:J1X301 4.8 11.9 0.9 HA A:ASN170 4.8 6.1 1.0 O A:HOH618 4.9 30.8 1.0 H A:ASP240 4.9 14.5 1.0 C A:THR171 4.9 11.3 1.0 HG2 A:PRO167 4.9 15.1 1.0 CG A:ASN170 5.0 10.9 1.0 OG1 A:THR171 5.0 7.5 1.0 ND2 A:ASN170 5.0 14.6 1.0

Fluorine binding site 2 out of 3 in the The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:15.0 occ:0.91 F08 A:J1X301 0.0 15.0 0.9 C06 A:J1X301 1.4 15.3 0.9 F07 A:J1X301 2.2 23.4 0.9 F09 A:J1X301 2.2 20.2 0.9 C05 A:J1X301 2.4 16.5 0.9 C04 A:J1X301 2.8 10.0 0.9 HB2 A:PRO167 2.9 10.5 1.0 HG2 A:PRO167 2.9 15.1 1.0 O A:PRO167 3.1 10.2 1.0 HA A:THR168 3.1 9.6 1.0 O A:HOH618 3.3 30.8 1.0 O A:HOH620 3.4 25.6 1.0 C A:PRO167 3.4 7.5 1.0 CB A:PRO167 3.6 8.8 1.0 C10 A:J1X301 3.7 10.2 0.9 CG A:PRO167 3.7 12.5 1.0 N A:THR168 3.9 8.5 1.0 CA A:THR168 3.9 8.0 1.0 O A:HOH555 4.0 25.0 1.0 HG22 A:THR168 4.0 16.5 1.0 HB2 A:ASN170 4.1 11.4 1.0 HG23 A:THR171 4.2 12.0 1.0 C03 A:J1X301 4.2 13.9 0.9 CA A:PRO167 4.2 8.9 1.0 HG3 A:PRO167 4.2 15.1 1.0 HG22 A:THR171 4.4 12.0 1.0 O A:HOH614 4.4 27.2 1.0 HB3 A:PRO167 4.4 10.5 1.0 H A:ASN170 4.5 8.4 1.0 HD22 A:ASN170 4.5 17.5 1.0 H A:THR168 4.5 10.2 1.0 CG2 A:THR171 4.7 10.0 1.0 CD A:PRO167 4.8 15.9 1.0 CG2 A:THR168 4.8 13.7 1.0 C A:THR168 4.8 8.4 1.0 HD2 A:PRO167 4.8 19.1 1.0 HA A:PRO167 4.8 10.7 1.0 C11 A:J1X301 4.8 18.2 0.9 HD21 A:ASN104 4.9 19.4 1.0 HD22 A:ASN104 4.9 19.4 1.0 HG23 A:THR168 4.9 16.5 1.0 O01 A:J1X301 4.9 10.8 0.9 CB A:THR168 4.9 7.1 1.0

Fluorine binding site 3 out of 3 in the The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Role of An Asp-Asp Pair in the Structure, Function and Inhibition of Ctx-M Class A Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:20.2 occ:0.91 F09 A:J1X301 0.0 20.2 0.9 C06 A:J1X301 1.4 15.3 0.9 F08 A:J1X301 2.2 15.0 0.9 F07 A:J1X301 2.2 23.4 0.9 C05 A:J1X301 2.3 16.5 0.9 O A:HOH614 2.7 27.2 1.0 C10 A:J1X301 2.7 10.2 0.9 O A:HOH410 3.2 28.6 1.0 HG22 A:THR171 3.5 12.0 1.0 C04 A:J1X301 3.6 10.0 0.9 O A:HOH618 3.9 30.8 1.0 O A:HOH620 4.0 25.6 1.0 HG23 A:THR171 4.1 12.0 1.0 HA A:THR171 4.1 14.2 1.0 C11 A:J1X301 4.1 18.2 0.9 CG2 A:THR171 4.2 10.0 1.0 HA A:THR168 4.5 9.6 1.0 O A:HOH555 4.6 25.0 1.0 C03 A:J1X301 4.7 13.9 0.9 HB2 A:ASP240 4.7 15.9 1.0 HG21 A:THR171 4.8 12.0 1.0 CA A:THR171 4.9 11.8 1.0 C17 A:J1X301 4.9 11.9 0.9 HB2 A:ASN170 4.9 11.4 1.0 O A:PRO167 4.9 10.2 1.0 C16 A:J1X301 4.9 14.1 0.9 N12 A:J1X301 4.9 22.7 0.9 HB2 A:PRO167 5.0 10.5 1.0

M.T.Kemp, D.A.Nichols, X.Zhang, K.Defrees, I.Na, A.R.Renslo, Y.Chen. Mutation of the Conserved Asp-Asp Pair Impairs the Structure, Function, and Inhibition of Ctx-M Class A Beta-Lactamase. Febs Lett. 2021.
ISSN: ISSN 0014-5793
PubMed: 34704263
DOI: 10.1002/1873-3468.14215