Atomistry » Zinc » PDB 1pe8-1pud » 1pfw
Atomistry »
  Zinc »
    PDB 1pe8-1pud »
      1pfw »

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 Dec 16 03:00:47 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy