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Zinc in PDB 6spq: Structure of the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine

Enzymatic activity of Structure of the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine

All present enzymatic activity of Structure of the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine:
6.1.1.10;

Protein crystallography data

The structure of Structure of the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine, PDB code: 6spq was solved by G.Nigro, E.Schmitt, Y.Mechulam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.53 / 1.38
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.420, 45.130, 86.150, 90.00, 107.49, 90.00
R / Rfree (%) 12.7 / 16.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine (pdb code 6spq). 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 the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine, PDB code: 6spq:

Zinc binding site 1 out of 1 in 6spq

Go back to Zinc Binding Sites List in 6spq
Zinc binding site 1 out of 1 in the Structure of the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Escherichia Coli Methionyl-Trna Synthetase Variant VI298 Complexed with Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:18.8
occ:1.00
 SG A:CYS161 2.3 20.1 1.0
SG A:CYS145 2.3 18.6 1.0
SG A:CYS148 2.3 18.2 1.0
SG A:CYS158 2.3 17.9 1.0
HB3 A:CYS158 3.0 23.0 1.0
CB A:CYS158 3.0 19.1 1.0
H A:CYS161 3.0 24.2 1.0
HB2 A:CYS158 3.0 23.0 1.0
HB3 A:CYS145 3.1 22.3 1.0
H A:CYS148 3.1 23.3 1.0
CB A:CYS145 3.1 18.6 1.0
HB3 A:CYS148 3.1 22.8 1.0
HB2 A:CYS145 3.1 22.3 1.0
HB3 A:CYS161 3.1 22.2 1.0
CB A:CYS148 3.3 19.0 1.0
CB A:CYS161 3.3 18.5 1.0
N A:CYS161 3.8 20.2 1.0
N A:CYS148 3.8 19.4 1.0
HB2 A:LYS147 3.8 29.2 0.9
HB2 A:SER150 3.8 22.8 1.0
HB3 A:ALA163 3.9 29.8 1.0
HB A:VAL160 4.0 24.3 1.0
CA A:CYS161 4.1 20.3 1.0
HB2 A:CYS148 4.1 22.8 1.0
H A:ALA163 4.1 28.4 1.0
CA A:CYS148 4.1 18.7 1.0
HB2 A:CYS161 4.1 22.2 1.0
H A:SER150 4.1 21.8 1.0
HB2 A:ALA163 4.5 29.8 1.0
H A:VAL160 4.5 23.9 1.0
H A:LYS147 4.5 24.5 1.0
HE2 A:TYR165 4.5 26.7 1.0
CA A:CYS158 4.5 19.3 1.0
H A:LYS149 4.5 22.4 1.0
H A:GLY162 4.5 26.3 1.0
CA A:CYS145 4.6 18.0 1.0
HG3 A:GLN153 4.6 22.6 1.0
CB A:ALA163 4.6 24.8 1.0
HG A:SER150 4.6 25.9 1.0
CB A:SER150 4.7 19.0 1.0
CB A:LYS147 4.7 24.4 1.0
C A:CYS161 4.7 20.3 1.0
C A:CYS148 4.8 19.5 1.0
N A:GLY162 4.9 21.9 1.0
HA A:CYS158 4.9 23.1 1.0
N A:LYS149 4.9 18.6 1.0
C A:LYS147 4.9 22.6 1.0
CB A:VAL160 4.9 20.3 1.0
HA A:CYS161 4.9 24.3 1.0
N A:ALA163 4.9 23.6 1.0
HA A:CYS148 4.9 22.5 1.0
C A:VAL160 4.9 20.9 1.0
OG A:SER150 4.9 21.6 1.0
HA A:CYS145 4.9 21.6 1.0
N A:SER150 5.0 18.1 1.0

Reference:

G.Nigro, S.Bourcier, C.Lazennec-Schurdevin, E.Schmitt, P.Marliere, Y.Mechulam. Use of BETA3-Methionine As An Amino Acid Substrate of Escherichia Coli Methionyl-Trna Synthetase. J.Struct.Biol. 07435 2019.
ISSN: ESSN 1095-8657
PubMed: 31862305
DOI: 10.1016/J.JSB.2019.107435
Page generated: Thu Aug 21 19:46:03 2025

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