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Zinc in PDB 1wke: Trna-Guanine Transglycosylase

Enzymatic activity of Trna-Guanine Transglycosylase

All present enzymatic activity of Trna-Guanine Transglycosylase:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase, PDB code: 1wke was solved by C.Romier, K.Reuter, D.Suck, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.200, 64.500, 72.000, 90.00, 96.90, 90.00
R / Rfree (%) 20.3 / 24.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (pdb code 1wke). 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 Trna-Guanine Transglycosylase, PDB code: 1wke:

Zinc binding site 1 out of 1 in 1wke

Go back to Zinc Binding Sites List in 1wke
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Trna-Guanine Transglycosylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:12.1
occ:1.00
SG A:CYS320 2.3 9.0 1.0
SG A:CYS323 2.3 13.8 1.0
SG A:CYS318 2.3 9.2 1.0
ND1 A:HIS349 2.4 4.3 1.0
CB A:CYS320 3.3 9.2 1.0
CE1 A:HIS349 3.3 5.9 1.0
CB A:CYS323 3.3 8.9 1.0
CB A:CYS318 3.3 13.0 1.0
CG A:HIS349 3.4 4.8 1.0
CB A:HIS349 3.8 3.6 1.0
N A:CYS323 3.9 12.8 1.0
N A:CYS320 4.0 15.2 1.0
CA A:CYS320 4.1 13.1 1.0
CA A:HIS349 4.1 6.3 1.0
CA A:CYS323 4.2 10.8 1.0
O A:CYS320 4.3 14.0 1.0
NE2 A:HIS349 4.4 7.0 1.0
C A:CYS320 4.5 12.2 1.0
CD2 A:HIS349 4.5 6.7 1.0
CA A:CYS318 4.6 16.5 1.0
O A:HIS349 4.6 7.0 1.0
C A:CYS318 4.7 19.0 1.0
O A:CYS318 4.7 17.6 1.0
CB A:VAL322 4.7 4.4 1.0
C A:HIS349 4.8 7.4 1.0
C A:VAL322 4.9 10.6 1.0

Reference:

C.Romier, K.Reuter, D.Suck, R.Ficner. Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna-Guanine Transglycosylase Reveal Aspartate 102 As the Active Site Nucleophile. Biochemistry V. 35 15734 1996.
ISSN: ISSN 0006-2960
PubMed: 8961936
DOI: 10.1021/BI962003N
Page generated: Wed Dec 16 03:09:52 2020

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