Zinc in PDB 6yfx: Tgt Y330F Mutant Crystallised at pH 5.5

Enzymatic activity of Tgt Y330F Mutant Crystallised at pH 5.5

All present enzymatic activity of Tgt Y330F Mutant Crystallised at pH 5.5:
2.4.2.29;

Protein crystallography data

The structure of Tgt Y330F Mutant Crystallised at pH 5.5, PDB code: 6yfx was solved by A.Nguyen, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.56 / 1.38
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 84.575, 65.066, 71.404, 90.00, 93.71, 90.00
R / Rfree (%) 14.1 / 16.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Tgt Y330F Mutant Crystallised at pH 5.5 (pdb code 6yfx). 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 Tgt Y330F Mutant Crystallised at pH 5.5, PDB code: 6yfx:

Zinc binding site 1 out of 1 in 6yfx

Go back to Zinc Binding Sites List in 6yfx
Zinc binding site 1 out of 1 in the Tgt Y330F Mutant Crystallised at pH 5.5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Tgt Y330F Mutant Crystallised at pH 5.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:18.9
occ:0.82
ND1 A:HIS349 2.2 17.7 1.0
SG A:CYS323 2.3 22.1 1.0
SG A:CYS318 2.3 23.3 1.0
SG A:CYS320 2.3 23.4 1.0
CE1 A:HIS349 2.9 19.1 1.0
HE1 A:HIS349 2.9 22.9 1.0
HB2 A:CYS323 3.0 28.5 1.0
HB3 A:CYS318 3.0 29.7 1.0
HB3 A:CYS320 3.1 30.1 1.0
CB A:CYS318 3.2 24.8 1.0
CB A:CYS323 3.3 23.8 1.0
CG A:HIS349 3.3 16.6 1.0
H A:CYS323 3.4 30.9 1.0
CB A:CYS320 3.4 25.2 1.0
HB2 A:HIS349 3.5 20.4 1.0
H A:CYS320 3.5 33.2 1.0
HA A:HIS349 3.6 20.5 1.0
HB2 A:CYS318 3.6 29.7 1.0
CB A:HIS349 3.8 17.1 1.0
HB A:VAL322 3.9 33.2 1.0
N A:CYS323 4.0 25.8 1.0
HB3 A:CYS323 4.0 28.5 1.0
HB2 A:CYS320 4.1 30.1 1.0
NE2 A:HIS349 4.1 17.4 1.0
N A:CYS320 4.2 27.7 1.0
CA A:HIS349 4.2 17.1 1.0
CA A:CYS323 4.2 25.5 1.0
CA A:CYS320 4.2 27.4 1.0
CD2 A:HIS349 4.3 17.0 1.0
HE22 A:GLN356 4.4 33.1 1.0
H A:ASP315 4.5 26.1 1.0
HB3 A:ASP315 4.5 29.0 1.0
O A:HIS349 4.6 17.9 1.0
CA A:CYS318 4.6 26.6 1.0
HA A:CYS323 4.6 30.6 1.0
HB3 A:ALA352 4.6 24.0 1.0
O A:CYS320 4.7 27.4 1.0
C A:CYS320 4.7 28.7 1.0
C A:CYS318 4.7 28.0 1.0
HB3 A:HIS349 4.7 20.4 1.0
CB A:VAL322 4.8 27.7 1.0
H A:VAL322 4.8 34.8 1.0
C A:HIS349 4.8 16.3 1.0
HE2 A:HIS349 4.9 20.9 1.0
O A:CYS318 4.9 28.8 1.0
C A:VAL322 5.0 26.7 1.0

Reference:

A.Nguyen, A.Heine, G.Klebe. Mutation Study on Trna-Guanine Transglycosylase For Catalysis Testing To Be Published.
Page generated: Wed Dec 16 13:15:56 2020

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