Zinc in PDB 4e30: X-Ray Structure of the H181N/E224Q Double Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp

The structure of X-Ray Structure of the H181N/E224Q Double Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp, PDB code: 4e30 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 / 1.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	100.660, 114.286, 37.857, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 21.8

The binding sites of Zinc atom in the X-Ray Structure of the H181N/E224Q Double Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp (pdb code 4e30). 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 H181N/E224Q Double Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Dtdp, PDB code: 4e30:

Zinc binding site 1 out of 1 in the X-Ray Structure of the H181N/E224Q Double 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 H181N/E224Q Double 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:20.8 occ:1.00 SG A:CYS16 2.2 21.9 1.0 SG A:CYS57 2.3 21.8 1.0 SG A:CYS13 2.3 18.4 1.0 SG A:CYS54 2.4 22.4 1.0 CB A:CYS54 3.2 15.0 1.0 CB A:CYS13 3.2 17.9 1.0 CB A:CYS57 3.3 22.7 1.0 CB A:CYS16 3.4 22.3 1.0 N A:CYS16 3.6 20.6 1.0 N A:CYS57 3.7 22.2 1.0 CA A:CYS57 4.0 21.9 1.0 CA A:CYS16 4.0 21.6 1.0 CB A:VAL15 4.4 22.2 1.0 N A:GLY18 4.4 28.7 1.0 C A:CYS16 4.6 25.1 1.0 N A:GLY17 4.6 21.7 1.0 CA A:CYS13 4.6 16.4 1.0 C A:VAL15 4.6 22.4 1.0 CA A:CYS54 4.6 16.4 1.0 CB A:SER56 4.7 28.0 1.0 C A:SER56 4.7 29.0 1.0 C A:CYS57 4.7 21.1 1.0 CA A:GLY18 4.8 26.4 1.0 CB A:MET59 4.8 13.3 1.0 N A:VAL15 4.8 17.6 1.0 CA A:VAL15 4.9 20.5 1.0 CG1 A:VAL15 4.9 23.8 1.0 N A:GLU58 4.9 18.9 1.0 N A:SER56 4.9 30.1 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