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Zinc in PDB 1pfw: Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine

Enzymatic activity of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine

All present enzymatic activity of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine:
6.1.1.10;

Protein crystallography data

The structure of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine, PDB code: 1pfw was solved by T.Crepin, E.Schmitt, Y.Mechulam, P.B.Sampson, M.D.Vaughan, J.F.Honek, S.Blanquet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.00 / 1.78
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.490, 45.288, 86.274, 90.00, 107.37, 90.00
R / Rfree (%) 18.4 / 20.9

Other elements in 1pfw:

The structure of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine (pdb code 1pfw). 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 Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine, PDB code: 1pfw:

Zinc binding site 1 out of 1 in 1pfw

Go back to Zinc Binding Sites List in 1pfw
Zinc binding site 1 out of 1 in the Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn552

b:18.1
occ:1.00
 SG A:CYS148 2.3 20.0 1.0
SG A:CYS145 2.4 18.1 1.0
SG A:CYS161 2.4 20.9 1.0
SG A:CYS158 2.4 18.9 1.0
CB A:CYS145 3.1 19.8 1.0
CB A:CYS158 3.1 20.6 1.0
CB A:CYS161 3.3 22.1 1.0
CB A:CYS148 3.4 22.0 1.0
N A:CYS148 3.7 21.6 1.0
N A:CYS161 3.7 23.2 1.0
CA A:CYS161 4.1 22.7 1.0
CA A:CYS148 4.1 22.3 1.0
CA A:CYS145 4.5 19.4 1.0
CA A:CYS158 4.6 21.1 1.0
CB A:LYS147 4.6 26.8 1.0
CB A:SER150 4.7 19.8 1.0
CB A:VAL160 4.7 22.8 1.0
C A:CYS148 4.8 22.5 1.0
C A:CYS161 4.8 23.1 1.0
CB A:ALA163 4.8 23.1 1.0
N A:LYS149 4.8 20.1 1.0
N A:GLY162 4.8 22.8 1.0
OG A:SER150 4.8 22.1 1.0
C A:LYS147 4.9 24.0 1.0
C A:VAL160 4.9 23.4 1.0
N A:SER150 4.9 19.0 1.0
N A:ALA163 5.0 21.7 1.0

Reference:

T.Crepin, E.Schmitt, Y.Mechulam, P.B.Sampson, M.D.Vaughan, J.F.Honek, S.Blanquet. Use of Analogues of Methionine and Methionyl Adenylate to Sample Conformational Changes During Catalysis in Escherichia Coli Methionyl-Trna Synthetase. J.Mol.Biol. V. 332 59 2003.
ISSN: ISSN 0022-2836
PubMed: 12946347
DOI: 10.1016/S0022-2836(03)00917-3
Page generated: Wed Oct 16 17:49:16 2024

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