Zinc in PDB 7bj9: Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A

All present enzymatic activity of Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A:
3.5.2.6;

The structure of Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A, PDB code: 7bj9 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)	72.06 / 1.21
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	33.083, 88.071, 72.061, 90, 90.51, 90
R / Rfree (%)	13.6 / 15.2

The binding sites of Zinc atom in the Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A (pdb code 7bj9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A, PDB code: 7bj9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:10.3 occ:1.00 OD2 B:ASP120 1.9 9.3 1.0 NE2 B:HIS263 2.1 9.1 1.0 H011 B:TWW402 2.1 16.0 1.0 S01 B:TWW402 2.3 13.3 1.0 SG B:CYS221 2.3 11.8 1.0 CE1 B:HIS263 3.0 9.3 1.0 CG B:ASP120 3.0 7.6 1.0 HB3 B:CYS221 3.1 13.9 1.0 HE1 B:HIS263 3.1 11.1 1.0 H021 B:TWW402 3.1 20.1 1.0 CD2 B:HIS263 3.2 8.7 1.0 O B:HOH513 3.2 33.3 1.0 C02 B:TWW402 3.2 16.8 1.0 CB B:CYS221 3.3 11.6 1.0 OD1 B:ASP120 3.3 10.6 1.0 HH21 B:ARG121 3.4 13.9 1.0 HD2 B:HIS263 3.4 10.4 1.0 H022 B:TWW402 3.4 20.1 1.0 NH2 B:ARG121 3.9 11.6 1.0 HB2 B:CYS221 4.0 13.9 1.0 HA B:CYS221 4.1 11.0 1.0 HE B:ARG121 4.1 9.7 1.0 ND1 B:HIS263 4.1 8.4 1.0 HE1 B:HIS196 4.2 14.1 1.0 CG B:HIS263 4.2 8.7 1.0 HH22 B:ARG121 4.3 13.9 1.0 CB B:ASP120 4.3 6.7 1.0 CA B:CYS221 4.3 9.2 1.0 HB2 B:ASP120 4.4 8.0 1.0 O B:HOH577 4.4 19.9 1.0 HB3 B:ASP120 4.5 8.0 1.0 CE1 B:HIS196 4.5 11.8 1.0 NE B:ARG121 4.5 8.1 1.0 CZ B:ARG121 4.5 8.4 1.0 O B:HOH643 4.6 12.4 1.0 HD21 B:ASN116 4.6 11.5 1.0 NE2 B:HIS196 4.6 11.7 1.0 O05 B:TWW402 4.7 17.7 1.0 H072 B:TWW402 4.7 23.6 1.0 HG2 B:ARG121 4.8 7.2 1.0 C03 B:TWW402 4.9 16.2 1.0 HD1 B:HIS263 4.9 10.1 1.0 C04 B:TWW402 5.0 18.1 1.0

Zinc binding site 2 out of 2 in the Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Sfh-I with 2-Mercaptomethyl-Thiazolidine L-Anti-1A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:12.5 occ:1.00 OD2 A:ASP120 1.9 12.2 1.0 NE2 A:HIS263 2.1 11.3 1.0 H011 A:TWW402 2.2 20.1 1.0 S01 A:TWW402 2.3 16.8 1.0 SG A:CYS221 2.4 14.0 1.0 CG A:ASP120 3.0 10.6 1.0 CE1 A:HIS263 3.0 11.8 1.0 HB3 A:CYS221 3.1 16.9 1.0 HE1 A:HIS263 3.1 14.2 1.0 CD2 A:HIS263 3.2 11.0 1.0 H022 A:TWW402 3.2 24.7 1.0 C02 A:TWW402 3.3 20.6 1.0 HH21 A:ARG121 3.3 15.4 1.0 CB A:CYS221 3.3 14.1 1.0 OD1 A:ASP120 3.3 12.1 1.0 HD2 A:HIS263 3.4 13.2 1.0 H021 A:TWW402 3.4 24.7 1.0 NH2 A:ARG121 3.8 12.8 1.0 HA A:CYS221 4.0 14.7 1.0 HB2 A:CYS221 4.0 16.9 1.0 HE A:ARG121 4.1 11.9 1.0 ND1 A:HIS263 4.1 11.3 1.0 HH22 A:ARG121 4.2 15.4 1.0 CB A:ASP120 4.2 9.9 1.0 CG A:HIS263 4.3 10.9 1.0 CA A:CYS221 4.3 12.3 1.0 HE1 A:HIS196 4.3 17.3 1.0 HB2 A:ASP120 4.4 11.8 1.0 O A:HOH549 4.5 19.4 1.0 HB3 A:ASP120 4.5 11.8 1.0 CZ A:ARG121 4.5 10.2 1.0 NE A:ARG121 4.5 9.9 1.0 CE1 A:HIS196 4.6 14.4 1.0 O A:HOH589 4.6 16.1 1.0 HD21 A:ASN116 4.6 12.5 1.0 NE2 A:HIS196 4.7 14.1 1.0 H073 A:TWW402 4.7 29.2 1.0 O05 A:TWW402 4.7 24.1 1.0 HG2 A:ARG121 4.8 9.8 1.0 HD1 A:HIS263 4.9 13.6 1.0 C03 A:TWW402 4.9 23.4 1.0 C04 A:TWW402 5.0 24.4 1.0

P.Hinchliffe, D.M.Moreno, M.A.Rossi, M.F.Mojica, V.Martinez, V.Villamil, B.Spellberg, G.L.Drusano, C.Banchio, G.Mahler, R.A.Bonomo, A.J.Vila, J.Spencer. 2-Mercaptomethyl Thiazolidines (Mmtzs) Inhibit All Metallo-Beta-Lactamase Classes By Maintaining A Conserved Binding Mode. Acs Infect Dis. 2021.
ISSN: ESSN 2373-8227
PubMed: 34355567
DOI: 10.1021/ACSINFECDIS.1C00194