Zinc in PDB 8brv: Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C Complexed with BETA3-Methionine.

Enzymatic activity of Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C Complexed with BETA3-Methionine.

All present enzymatic activity of Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C Complexed with BETA3-Methionine.:
6.1.1.10;

Protein crystallography data

The structure of Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C Complexed with BETA3-Methionine., PDB code: 8brv 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) 48.68 / 1.53
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.65, 45.47, 86.47, 90, 107.5, 90
R / Rfree (%) 15.1 / 19.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C Complexed with BETA3-Methionine. (pdb code 8brv). 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 Complexed with BETA3-Methionine., PDB code: 8brv:

Zinc binding site 1 out of 1 in 8brv

Go back to Zinc Binding Sites List in 8brv
Zinc binding site 1 out of 1 in the Escherichia Coli Methionyl-Trna Synthetase Mutant L13M,I297C Complexed with BETA3-Methionine.


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 Complexed with BETA3-Methionine. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:22.1
occ:1.00
 SG A:CYS145 2.2 21.7 1.0
SG A:CYS148 2.3 22.1 1.0
SG A:CYS161 2.4 23.0 1.0
SG A:CYS158 2.4 21.0 1.0
HB3 A:CYS158 3.0 23.8 1.0
H A:CYS148 3.0 28.5 1.0
HB3 A:CYS145 3.0 26.0 1.0
CB A:CYS145 3.0 21.6 1.0
HB3 A:CYS148 3.1 29.5 1.0
CB A:CYS158 3.1 19.8 1.0
H A:CYS161 3.1 27.8 1.0
HB2 A:CYS145 3.1 26.0 1.0
HB2 A:CYS158 3.1 23.8 1.0
HB3 A:CYS161 3.1 23.7 1.0
CB A:CYS148 3.3 24.6 1.0
CB A:CYS161 3.4 19.7 1.0
N A:CYS148 3.8 23.7 1.0
HB2 A:LYS147 3.8 34.0 1.0
HB2 A:SER150 3.8 30.0 1.0
N A:CYS161 3.8 23.1 1.0
HB A:VAL160 3.9 28.1 1.0
HB3 A:ALA163 4.0 30.8 1.0
HB2 A:CYS148 4.0 29.5 1.0
H A:SER150 4.1 25.5 1.0
CA A:CYS148 4.1 22.8 1.0
CA A:CYS161 4.1 22.9 1.0
HB2 A:CYS161 4.1 23.7 1.0
H A:ALA163 4.1 29.1 1.0
H A:LYS147 4.4 29.9 1.0
H A:LYS149 4.5 25.1 1.0
H A:VAL160 4.5 27.2 1.0
HG A:SER150 4.5 31.0 1.0
CA A:CYS145 4.5 19.6 1.0
HB2 A:ALA163 4.5 30.8 1.0
CA A:CYS158 4.5 21.4 1.0
HE2 A:TYR165 4.6 26.6 1.0
H A:GLY162 4.6 25.2 1.0
HG3 A:GLN153 4.6 25.1 1.0
CB A:SER150 4.7 25.0 1.0
CB A:ALA163 4.7 25.6 1.0
C A:CYS148 4.7 20.9 1.0
CB A:LYS147 4.7 28.3 1.0
C A:CYS161 4.8 21.0 1.0
OG A:SER150 4.8 25.8 1.0
N A:LYS149 4.8 20.9 1.0
CB A:VAL160 4.9 23.4 1.0
HA A:CYS145 4.9 23.5 1.0
N A:GLY162 4.9 21.0 1.0
C A:LYS147 4.9 26.1 1.0
HA A:CYS148 4.9 27.3 1.0
N A:SER150 4.9 21.2 1.0
HA A:CYS158 4.9 25.6 1.0
HA A:CYS161 4.9 27.5 1.0
N A:ALA163 5.0 24.3 1.0
C A:VAL160 5.0 22.8 1.0

Reference:

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
Page generated: Wed Oct 30 18:25:33 2024

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