Zinc in PDB 3h9c: Structure of Methionyl-Trna Synthetase: Crystal Form 2

All present enzymatic activity of Structure of Methionyl-Trna Synthetase: Crystal Form 2:
6.1.1.10;

The structure of Structure of Methionyl-Trna Synthetase: Crystal Form 2, PDB code: 3h9c was solved by E.Schmitt, I.C.Tanrikulu, T.H.Yoo, M.Panvert, D.A.Tirrell, Y.Mechulam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.54 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.890, 45.400, 86.210, 90.00, 107.30, 90.00
R / Rfree (%)	16.5 / 19.1

The binding sites of Zinc atom in the Structure of Methionyl-Trna Synthetase: Crystal Form 2 (pdb code 3h9c). 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 Methionyl-Trna Synthetase: Crystal Form 2, PDB code: 3h9c:

Zinc binding site 1 out of 1 in the Structure of Methionyl-Trna Synthetase: Crystal Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Methionyl-Trna Synthetase: Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:9.8 occ:1.00 SG A:CYS161 2.3 10.5 1.0 SG A:CYS145 2.3 9.2 1.0 SG A:CYS148 2.4 10.7 1.0 SG A:CYS158 2.4 9.2 1.0 CB A:CYS158 3.1 11.5 1.0 CB A:CYS145 3.1 10.4 1.0 CB A:CYS161 3.3 9.8 1.0 CB A:CYS148 3.3 13.0 1.0 N A:CYS161 3.8 10.1 1.0 N A:CYS148 3.8 10.3 1.0 CA A:CYS161 4.1 12.0 1.0 CA A:CYS148 4.1 11.6 1.0 CA A:CYS145 4.6 9.3 1.0 CA A:CYS158 4.6 11.9 1.0 CB A:ALA163 4.7 14.1 1.0 CB A:LYS147 4.7 14.1 1.0 CB A:SER150 4.7 10.2 1.0 C A:CYS161 4.7 11.7 1.0 C A:CYS148 4.8 12.1 1.0 N A:GLY162 4.8 11.8 1.0 N A:LYS149 4.8 8.7 1.0 CB A:VAL160 4.8 10.0 1.0 OG A:SER150 4.9 12.2 1.0 C A:LYS147 4.9 14.1 1.0 C A:VAL160 4.9 13.1 1.0 N A:ALA163 4.9 12.4 1.0 N A:SER150 5.0 9.0 1.0

E.Schmitt, I.C.Tanrikulu, T.H.Yoo, M.Panvert, D.A.Tirrell, Y.Mechulam. Switching From An Induced-Fit to A Lock-and-Key Mechanism in An Aminoacyl-Trna Synthetase with Modified Specificity. J.Mol.Biol. V. 394 843 2009.
ISSN: ISSN 0022-2836
PubMed: 19837083
DOI: 10.1016/J.JMB.2009.10.016