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Zinc in PDB 4e2z: X-Ray Structure of the H225N Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product

Protein crystallography data

The structure of X-Ray Structure of the H225N Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product, PDB code: 4e2z 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 / 1.41
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 102.039, 114.280, 38.038, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 21.7

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Structure of the H225N Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product (pdb code 4e2z). 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 H225N Mutant of TCAB9, A C-3'- Methyltransferase, in Complex with S-Adenosyl-L-Homocysteine and Sugar Product, PDB code: 4e2z:

Zinc binding site 1 out of 1 in 4e2z

Go back to Zinc Binding Sites List in 4e2z
Zinc binding site 1 out of 1 in the X-Ray Structure of the H225N 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 H225N 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:17.3
occ:1.00
SG A:CYS57 2.3 16.6 1.0
SG A:CYS16 2.3 18.5 1.0
SG A:CYS13 2.3 14.8 1.0
SG A:CYS54 2.4 16.9 1.0
CB A:CYS54 3.1 10.3 1.0
CB A:CYS13 3.1 13.9 1.0
CB A:CYS57 3.3 20.1 1.0
CB A:CYS16 3.4 17.5 1.0
N A:CYS57 3.7 17.3 1.0
N A:CYS16 3.8 17.8 1.0
CA A:CYS57 4.1 15.4 1.0
CA A:CYS16 4.1 19.8 1.0
N A:GLY18 4.5 20.5 1.0
CA A:CYS54 4.6 15.9 1.0
CB A:VAL15 4.6 17.5 1.0
CA A:CYS13 4.6 15.8 1.0
C A:CYS16 4.6 21.4 1.0
CB A:SER56 4.7 23.7 1.0
C A:CYS57 4.7 18.4 1.0
C A:SER56 4.7 24.2 1.0
N A:GLY17 4.8 17.8 1.0
C A:VAL15 4.8 20.2 1.0
CB A:MET59 4.8 9.3 1.0
CA A:GLY18 4.8 21.0 1.0
N A:SER56 4.9 22.0 1.0
N A:GLU58 5.0 13.8 1.0
N A:VAL15 5.0 16.3 1.0

Reference:

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
Page generated: Sat Oct 26 21:50:26 2024

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