Zinc in PDB 8of9: Structure of TEM1 Beta-Lactamase Variant 70.A

All present enzymatic activity of Structure of TEM1 Beta-Lactamase Variant 70.A:
3.5.2.6;

The structure of Structure of TEM1 Beta-Lactamase Variant 70.A, PDB code: 8of9 was solved by E.Napier, B.F.Fram, N.P.J.Gauthier, C.Sander, A.R.Khan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.22 / 3.11
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	114.972, 114.972, 49.181, 90, 90, 90
R / Rfree (%)	21.8 / 26.7

The binding sites of Zinc atom in the Structure of TEM1 Beta-Lactamase Variant 70.A (pdb code 8of9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of TEM1 Beta-Lactamase Variant 70.A, PDB code: 8of9:

Zinc binding site 1 out of 1 in the Structure of TEM1 Beta-Lactamase Variant 70.A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of TEM1 Beta-Lactamase Variant 70.A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:76.5 occ:1.00 OD2 A:ASP115 2.2 60.1 1.0 ND1 A:HIS112 2.3 63.0 1.0 OD1 A:ASP115 2.5 74.1 1.0 CG A:ASP115 2.5 64.5 1.0 HB3 A:HIS112 2.9 65.4 1.0 CG A:HIS112 3.2 58.0 1.0 CE1 A:HIS112 3.3 85.9 1.0 HA A:HIS112 3.4 76.7 1.0 HE1 A:HIS112 3.4 103.0 1.0 CB A:HIS112 3.5 54.5 1.0 CB A:ASP115 3.9 68.3 1.0 CA A:HIS112 4.0 64.0 1.0 HB3 A:ASP115 4.1 81.9 1.0 O A:LYS111 4.1 80.2 1.0 HB2 A:ASP115 4.2 81.9 1.0 HB2 A:HIS112 4.4 65.4 1.0 NE2 A:HIS112 4.4 72.1 1.0 CD2 A:HIS112 4.4 63.9 1.0 H A:ASP115 4.6 90.7 1.0 O A:GLY116 4.8 78.8 1.0 N A:HIS112 4.8 56.3 1.0 C A:LYS111 4.9 51.6 1.0

B.Fram, I.Truebridge, Y.Su, A.J.Riesselman, J.B.Ingraham, A.Passera, E.Napier, N.N.Thadani, S.Lim, K.Roberts, G.Kaur, M.Stiffler, D.S.Marks, C.D.Bahl, A.R.Khan, C.Sander, N.P.Gauthier. Simultaneous Enhancement of Multiple Functional Properties Using Evolution-Informed Protein Design. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 37214973
DOI: 10.1101/2023.05.09.539914