Zinc in PDB 4e32: X-Ray Structure of the C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Dtdp-Sugar Substrate

The structure of X-Ray Structure of the C-3'-Methyltransferase TCAB9 in Complex with S- Adenosyl-L-Homocysteine and Dtdp-Sugar Substrate, PDB code: 4e32 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)	29.00 / 1.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	100.741, 114.383, 37.725, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.8

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 Dtdp-Sugar Substrate (pdb code 4e32). 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 Dtdp-Sugar Substrate, PDB code: 4e32:

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 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 Dtdp-Sugar Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:12.8 occ:1.00 SG A:CYS57 2.3 12.7 1.0 SG A:CYS16 2.3 15.4 1.0 SG A:CYS13 2.3 11.8 1.0 SG A:CYS54 2.4 12.9 1.0 CB A:CYS13 3.1 11.0 1.0 CB A:CYS54 3.2 9.3 1.0 CB A:CYS57 3.3 13.7 1.0 CB A:CYS16 3.4 13.9 1.0 N A:CYS57 3.6 15.7 1.0 N A:CYS16 3.8 13.5 1.0 CA A:CYS57 4.0 13.8 1.0 CA A:CYS16 4.1 13.6 1.0 CB A:VAL15 4.4 13.7 1.0 N A:GLY18 4.4 15.3 1.0 CA A:CYS13 4.5 11.9 1.0 CA A:CYS54 4.6 9.7 1.0 N A:GLY17 4.6 12.7 1.0 C A:CYS16 4.7 16.4 1.0 C A:SER56 4.7 19.9 1.0 C A:CYS57 4.7 13.6 1.0 CB A:MET59 4.7 8.6 1.0 C A:VAL15 4.7 15.5 1.0 CB A:SER56 4.8 17.9 1.0 CA A:GLY18 4.8 15.8 1.0 N A:GLU58 4.9 12.7 1.0 CA A:VAL15 4.9 13.1 1.0 N A:SER56 4.9 15.6 1.0 N A:VAL15 4.9 12.1 1.0 N A:MET59 5.0 7.4 1.0 NE2 A:GLN61 5.0 8.8 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