Zinc in PDB 4e2y: X-Ray Structure of the E224Q Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product

The structure of X-Ray Structure of the E224Q Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product, PDB code: 4e2y was solved by N.A.Bruender, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.00 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	100.365, 114.991, 38.020, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.8

The binding sites of Zinc atom in the X-Ray Structure of the E224Q Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product (pdb code 4e2y). 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 X-Ray Structure of the E224Q Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product, PDB code: 4e2y:

Zinc binding site 1 out of 1 in the X-Ray Structure of the E224Q Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of the E224Q Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:16.5 occ:1.00 SG A:CYS57 2.3 15.4 1.0 SG A:CYS16 2.3 18.0 1.0 SG A:CYS54 2.3 17.3 1.0 SG A:CYS13 2.3 14.3 1.0 CB A:CYS13 3.1 15.3 1.0 CB A:CYS54 3.1 12.5 1.0 CB A:CYS57 3.2 17.3 1.0 CB A:CYS16 3.4 15.6 1.0 N A:CYS16 3.7 16.2 1.0 N A:CYS57 3.8 16.9 1.0 CA A:CYS16 4.1 17.4 1.0 CA A:CYS57 4.1 16.7 1.0 CB A:VAL15 4.4 19.1 1.0 N A:GLY18 4.5 16.9 1.0 CA A:CYS13 4.6 14.3 1.0 CA A:CYS54 4.6 14.1 1.0 C A:CYS16 4.6 18.0 1.0 CB A:SER56 4.6 22.1 1.0 CB A:MET59 4.7 11.0 1.0 C A:VAL15 4.7 19.4 1.0 C A:CYS57 4.7 16.7 1.0 N A:GLY17 4.7 16.0 1.0 CA A:GLY18 4.8 17.3 1.0 N A:VAL15 4.9 15.7 1.0 C A:SER56 4.9 21.7 1.0 N A:GLU58 4.9 14.1 1.0 CA A:VAL15 4.9 18.6 1.0 CG1 A:VAL15 4.9 22.2 1.0 N A:SER56 5.0 19.9 1.0 NE2 A:GLN61 5.0 13.3 1.0

N.A.Bruender, H.M.Holden. Probing the Catalytic Mechanism of A C-3'-Methyltransferase Involved in the Biosynthesis of D-Tetronitrose. Protein Sci. V. 21 876 2012.
ISSN: ISSN 0961-8368
PubMed: 22495991
DOI: 10.1002/PRO.2074