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Zinc in PDB 1pud: 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: 1pud 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) 8.00 / 1.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.100, 65.100, 71.900, 90.00, 97.50, 90.00
R / Rfree (%) 19 / 21.4

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 1pud

Go back to Zinc Binding Sites List in 1pud
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:12.6
occ:1.00
ND1 A:HIS349 2.1 8.8 1.0
SG A:CYS323 2.1 19.8 1.0
SG A:CYS320 2.2 10.8 1.0
SG A:CYS318 2.3 12.0 1.0
CE1 A:HIS349 2.9 8.9 1.0
CG A:HIS349 3.2 6.8 1.0
CB A:CYS318 3.3 16.2 1.0
CB A:CYS323 3.3 10.6 1.0
CB A:CYS320 3.4 9.4 1.0
CB A:HIS349 3.7 7.5 1.0
N A:CYS323 4.0 8.9 1.0
CA A:HIS349 4.1 6.2 1.0
NE2 A:HIS349 4.1 10.5 1.0
N A:CYS320 4.2 12.8 1.0
CD2 A:HIS349 4.3 5.8 1.0
CA A:CYS323 4.3 12.3 1.0
CA A:CYS320 4.3 11.3 1.0
O A:HIS349 4.5 7.5 1.0
CA A:CYS318 4.6 18.0 1.0
O A:CYS320 4.6 11.3 1.0
C A:CYS318 4.7 18.0 1.0
C A:CYS320 4.7 10.4 1.0
C A:HIS349 4.7 7.9 1.0
O A:CYS318 4.8 16.2 1.0
CB A:VAL322 4.9 9.4 1.0
CB A:LEU314 5.0 12.4 1.0

Reference:

C.Romier, K.Reuter, D.Suck, R.Ficner. Crystal Structure of Trna-Guanine Transglycosylase: Rna Modification By Base Exchange. Embo J. V. 15 2850 1996.
ISSN: ISSN 0261-4189
PubMed: 8654383
Page generated: Wed Dec 16 03:01:03 2020

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