Zinc in PDB 4e2x: X-Ray Structure of the Y222F Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp

The structure of X-Ray Structure of the Y222F Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp, PDB code: 4e2x 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 / 1.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	100.542, 114.174, 37.632, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 23.6

The binding sites of Zinc atom in the X-Ray Structure of the Y222F Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp (pdb code 4e2x). 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 Y222F Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp, PDB code: 4e2x:

Zinc binding site 1 out of 1 in the X-Ray Structure of the Y222F Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp


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 Y222F Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:12.2 occ:1.00 SG A:CYS16 2.3 12.9 1.0 SG A:CYS57 2.3 12.0 1.0 SG A:CYS13 2.3 10.1 1.0 SG A:CYS54 2.4 11.9 1.0 CB A:CYS13 3.1 10.3 1.0 CB A:CYS54 3.1 9.6 1.0 CB A:CYS57 3.2 13.1 1.0 CB A:CYS16 3.5 12.2 1.0 N A:CYS16 3.7 12.0 1.0 N A:CYS57 3.7 14.1 1.0 CA A:CYS57 4.0 11.6 1.0 CA A:CYS16 4.1 12.6 1.0 N A:GLY18 4.4 14.8 1.0 CB A:VAL15 4.4 13.4 1.0 CA A:CYS13 4.5 10.6 1.0 CA A:CYS54 4.6 14.5 1.0 CA A:GLY18 4.7 15.7 1.0 C A:VAL15 4.7 12.5 1.0 C A:CYS16 4.7 15.1 1.0 CB A:SER56 4.7 16.3 1.0 N A:GLY17 4.7 15.5 1.0 C A:CYS57 4.7 10.2 1.0 C A:SER56 4.7 17.8 1.0 CB A:MET59 4.8 9.1 1.0 CA A:VAL15 4.9 12.9 1.0 N A:SER56 4.9 15.8 1.0 N A:VAL15 4.9 12.9 1.0 N A:GLU58 4.9 12.6 1.0 CG1 A:VAL15 4.9 15.7 1.0 NE2 A:GLN61 5.0 9.0 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