Zinc in PDB 8bru: Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C

All present enzymatic activity of Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C:
6.1.1.10;

The structure of Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C, PDB code: 8bru was solved by E.Schmitt, Y.Mechulam, G.Nigro, V.Opuu, C.Lazennec-Schurdevin, T.Simonson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.00 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.31, 45.08, 86.17, 90, 107.54, 90
R / Rfree (%)	14.4 / 18.1

The binding sites of Zinc atom in the Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C (pdb code 8bru). 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 Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C, PDB code: 8bru:

Zinc binding site 1 out of 1 in the Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:23.1 occ:1.00 SG A:CYS145 2.3 22.5 1.0 SG A:CYS148 2.3 23.0 1.0 SG A:CYS161 2.3 25.0 1.0 SG A:CYS158 2.4 21.9 1.0 HB3 A:CYS158 2.9 30.6 1.0 H A:CYS161 3.0 29.7 1.0 H A:CYS148 3.0 30.9 1.0 CB A:CYS158 3.0 25.5 1.0 HB3 A:CYS145 3.0 26.6 1.0 CB A:CYS145 3.1 22.2 1.0 HB2 A:CYS145 3.1 26.6 1.0 HB2 A:CYS158 3.1 30.6 1.0 HB3 A:CYS161 3.1 27.1 1.0 HB3 A:CYS148 3.2 28.1 1.0 CB A:CYS161 3.3 22.6 1.0 CB A:CYS148 3.3 23.4 1.0 N A:CYS161 3.7 24.8 1.0 HB2 A:LYS147 3.8 34.9 1.0 N A:CYS148 3.8 25.8 1.0 HB2 A:SER150 3.9 30.2 1.0 HB A:VAL160 3.9 31.8 1.0 HB3 A:ALA163 3.9 34.2 1.0 CA A:CYS161 4.1 25.2 1.0 CA A:CYS148 4.1 23.9 1.0 H A:ALA163 4.1 31.8 1.0 H A:SER150 4.1 26.9 1.0 HB2 A:CYS161 4.1 27.1 1.0 HB2 A:CYS148 4.1 28.1 1.0 H A:LYS147 4.4 30.9 1.0 H A:LYS149 4.4 26.0 1.0 H A:VAL160 4.4 27.2 1.0 HE2 A:TYR165 4.5 27.9 1.0 H A:GLY162 4.5 30.4 1.0 CA A:CYS158 4.5 24.2 1.0 HB2 A:ALA163 4.5 34.2 1.0 CA A:CYS145 4.5 19.3 1.0 HG A:SER150 4.6 35.4 1.0 HG3 A:GLN153 4.6 27.9 1.0 CB A:ALA163 4.7 28.6 1.0 CB A:LYS147 4.7 29.1 1.0 C A:CYS161 4.7 24.8 1.0 C A:CYS148 4.7 22.5 1.0 CB A:SER150 4.8 25.2 1.0 N A:LYS149 4.8 21.7 1.0 N A:GLY162 4.8 25.4 1.0 CB A:VAL160 4.9 26.5 1.0 HA A:CYS145 4.9 23.2 1.0 HA A:CYS158 4.9 29.1 1.0 C A:LYS147 4.9 27.7 1.0 HA A:CYS161 4.9 30.2 1.0 C A:VAL160 4.9 23.0 1.0 N A:ALA163 4.9 26.5 1.0 OG A:SER150 4.9 29.5 1.0 HA A:CYS148 4.9 28.6 1.0 N A:SER150 4.9 22.4 1.0

V.Opuu, G.Nigro, C.Lazennec-Schurdevin, Y.Mechulam, E.Schmitt, T.Simonson. Redesigning Methionyl-Trna Synthetase For Beta-Methionine Activity with Adaptive Landscape Flattening and Experiments. Protein Sci. E4738 2023.
ISSN: ESSN 1469-896X
PubMed: 37518893
DOI: 10.1002/PRO.4738