Zinc in PDB 4e33: X-Ray Structure of the C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Reduced Dtdp-Sugar Substrate

The structure of X-Ray Structure of the C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Reduced Dtdp-Sugar Substrate, PDB code: 4e33 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)	38.00 / 1.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	100.707, 114.367, 37.761, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.3

The binding sites of Zinc atom in the X-Ray Structure of the C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Reduced Dtdp-Sugar Substrate (pdb code 4e33). 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 C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Reduced Dtdp-Sugar Substrate, PDB code: 4e33:

Zinc binding site 1 out of 1 in the X-Ray Structure of the C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Reduced Dtdp-Sugar Substrate


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 C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Reduced Dtdp-Sugar Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:14.1 occ:1.00 SG A:CYS57 2.2 14.7 1.0 SG A:CYS13 2.3 12.9 1.0 SG A:CYS16 2.4 17.0 1.0 SG A:CYS54 2.4 14.5 1.0 CB A:CYS54 3.1 10.6 1.0 CB A:CYS13 3.2 14.2 1.0 CB A:CYS57 3.2 17.4 1.0 CB A:CYS16 3.5 16.3 1.0 N A:CYS57 3.6 16.1 1.0 N A:CYS16 3.8 17.7 1.0 CA A:CYS57 4.0 13.7 1.0 CA A:CYS16 4.1 17.6 1.0 CB A:VAL15 4.3 16.8 1.0 N A:GLY18 4.5 16.8 1.0 CA A:CYS54 4.6 10.6 1.0 C A:CYS16 4.6 18.4 1.0 CA A:CYS13 4.6 13.7 1.0 N A:GLY17 4.7 16.8 1.0 C A:CYS57 4.7 15.2 1.0 C A:VAL15 4.7 16.7 1.0 C A:SER56 4.7 17.9 1.0 CB A:MET59 4.7 10.9 1.0 CB A:SER56 4.8 21.1 1.0 CG1 A:VAL15 4.8 17.4 1.0 CA A:GLY18 4.8 17.6 1.0 N A:GLU58 4.9 11.0 1.0 N A:VAL15 4.9 14.2 1.0 CA A:VAL15 4.9 15.6 1.0 N A:SER56 4.9 19.6 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