Zinc in PDB 1qqt: Methionyl-Trna Synthetase From Escherichia Coli

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

The structure of Methionyl-Trna Synthetase From Escherichia Coli, PDB code: 1qqt was solved by Y.Mechulam, E.Schmitt, L.Maveyraud, C.Zelwer, O.Nureki, S.Yokoyama, M.Konno, S.Blanquet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.03
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.150, 46.300, 87.700, 90.00, 109.06, 90.00
R / Rfree (%)	17 / 21.4

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

Zinc binding site 1 out of 1 in the Methionyl-Trna Synthetase From Escherichia Coli


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn552 b:32.9 occ:1.00 SG A:CYS145 2.6 28.8 1.0 SG A:CYS158 2.6 32.2 1.0 SG A:CYS148 2.7 34.9 1.0 SG A:CYS161 2.8 42.8 1.0 CB A:CYS158 3.2 30.9 1.0 CB A:CYS145 3.2 28.5 1.0 CB A:CYS161 3.3 37.8 1.0 CB A:CYS148 3.4 36.9 1.0 N A:CYS148 3.7 38.1 1.0 N A:CYS161 3.7 35.4 1.0 CA A:CYS161 4.0 35.9 1.0 CA A:CYS148 4.1 39.2 1.0 CB A:LYS147 4.4 44.5 1.0 CB A:VAL160 4.6 33.0 1.0 CB A:ALA163 4.6 39.7 1.0 C A:CYS161 4.7 35.3 1.0 CA A:CYS158 4.7 32.0 1.0 CA A:CYS145 4.7 31.6 1.0 N A:GLY162 4.7 35.3 1.0 C A:LYS147 4.8 39.9 1.0 CB A:SER150 4.8 39.2 1.0 N A:ALA163 4.8 38.7 1.0 C A:CYS148 4.8 39.8 1.0 C A:VAL160 4.9 35.2 1.0 N A:LYS149 4.9 40.2 1.0 OG A:SER150 4.9 43.4 1.0 CA A:LYS147 5.0 41.8 1.0

Y.Mechulam, E.Schmitt, L.Maveyraud, C.Zelwer, O.Nureki, S.Yokoyama, M.Konno, S.Blanquet. Crystal Structure of Escherichia Coli Methionyl-Trna Synthetase Highlights Species-Specific Features. J.Mol.Biol. V. 294 1287 1999.
ISSN: ISSN 0022-2836
PubMed: 10600385
DOI: 10.1006/JMBI.1999.3339