Zinc in PDB 8brx: Escherichia Coli Methionyl-Trna Synthetase Mutant L13C,I297C Complexed with Beta-3-Methionine

Enzymatic activity of Escherichia Coli Methionyl-Trna Synthetase Mutant L13C,I297C Complexed with Beta-3-Methionine

All present enzymatic activity of Escherichia Coli Methionyl-Trna Synthetase Mutant L13C,I297C Complexed with Beta-3-Methionine:
6.1.1.10;

Protein crystallography data

The structure of Escherichia Coli Methionyl-Trna Synthetase Mutant L13C,I297C Complexed with Beta-3-Methionine, PDB code: 8brx 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) 41.82 / 1.54
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.66, 45.51, 86.43, 90, 107.51, 90
R / Rfree (%) 16.5 / 19.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Escherichia Coli Methionyl-Trna Synthetase Mutant L13C,I297C Complexed with Beta-3-Methionine (pdb code 8brx). 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 L13C,I297C Complexed with Beta-3-Methionine, PDB code: 8brx:

Zinc binding site 1 out of 1 in 8brx

Go back to Zinc Binding Sites List in 8brx
Zinc binding site 1 out of 1 in the Escherichia Coli Methionyl-Trna Synthetase Mutant L13C,I297C Complexed with Beta-3-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 L13C,I297C Complexed with Beta-3-Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:18.1
occ:1.00
 SG A:CYS161 2.3 18.4 1.0
SG A:CYS158 2.3 16.9 1.0
SG A:CYS145 2.3 16.8 1.0
SG A:CYS148 2.4 17.2 1.0
HB3 A:CYS158 3.0 21.9 1.0
HB3 A:CYS145 3.0 19.1 1.0
CB A:CYS158 3.0 18.3 1.0
H A:CYS161 3.1 22.0 1.0
CB A:CYS145 3.1 15.9 1.0
H A:CYS148 3.1 22.5 1.0
HB2 A:CYS158 3.1 21.9 1.0
HB2 A:CYS145 3.1 19.1 1.0
HB3 A:CYS148 3.1 22.0 1.0
HB3 A:CYS161 3.1 21.6 1.0
CB A:CYS161 3.3 18.0 1.0
CB A:CYS148 3.3 18.4 1.0
HB2 A:LYS147 3.8 28.8 1.0
N A:CYS161 3.8 18.3 1.0
N A:CYS148 3.8 18.8 1.0
HB2 A:SER150 3.9 22.7 1.0
HB A:VAL160 3.9 24.4 1.0
HB3 A:ALA163 3.9 25.5 1.0
HB2 A:CYS161 4.1 21.6 1.0
CA A:CYS161 4.1 17.4 1.0
H A:ALA163 4.1 25.9 1.0
H A:SER150 4.1 20.2 1.0
HB2 A:CYS148 4.1 22.0 1.0
CA A:CYS148 4.1 19.2 1.0
H A:VAL160 4.4 24.1 1.0
H A:LYS149 4.5 19.8 1.0
H A:LYS147 4.5 24.4 1.0
HB2 A:ALA163 4.5 25.5 1.0
HE2 A:TYR165 4.5 20.5 1.0
CA A:CYS158 4.5 18.6 1.0
CA A:CYS145 4.6 15.6 1.0
H A:GLY162 4.6 22.2 1.0
HG3 A:GLN153 4.6 19.2 1.0
HG A:SER150 4.6 25.5 1.0
CB A:ALA163 4.7 21.3 1.0
CB A:LYS147 4.7 24.0 1.0
CB A:SER150 4.8 18.9 1.0
C A:CYS148 4.8 18.1 1.0
C A:CYS161 4.8 18.0 1.0
N A:LYS149 4.8 16.5 1.0
CB A:VAL160 4.8 20.3 1.0
N A:GLY162 4.9 18.5 1.0
HA A:CYS158 4.9 22.3 1.0
HA A:CYS145 4.9 18.7 1.0
OG A:SER150 4.9 21.2 1.0
HA A:CYS161 4.9 20.9 1.0
N A:ALA163 4.9 21.6 1.0
C A:LYS147 4.9 20.8 1.0
C A:VAL160 4.9 17.9 1.0
N A:SER150 5.0 16.8 1.0
HA A:CYS148 5.0 23.0 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 18:25:42 2024

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