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Zinc in PDB 1enu: A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase

Enzymatic activity of A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase

All present enzymatic activity of A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase:
2.4.2.29;

Protein crystallography data

The structure of A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase, PDB code: 1enu was solved by U.Gradler, H.D.Gerber, D.M.Goodenough-Lashua, G.A.Garcia, R.Ficner, K.Reuter, M.T.Stubbs, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.790, 64.960, 70.420, 90.00, 96.47, 90.00
R / Rfree (%) 17.6 / 21.1

Zinc Binding Sites:

The binding sites of Zinc atom in the A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase (pdb code 1enu). 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 A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase, PDB code: 1enu:

Zinc binding site 1 out of 1 in 1enu

Go back to Zinc Binding Sites List in 1enu
Zinc binding site 1 out of 1 in the A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of 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 A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:17.9
occ:1.00
 SG A:CYS323 2.2 18.5 1.0
ND1 A:HIS349 2.2 15.1 1.0
SG A:CYS320 2.2 14.5 1.0
SG A:CYS318 2.3 15.4 1.0
CE1 A:HIS349 3.1 16.4 1.0
CG A:HIS349 3.3 14.2 1.0
CB A:CYS318 3.3 13.7 1.0
CB A:CYS323 3.3 15.4 1.0
CB A:CYS320 3.4 13.8 1.0
CB A:HIS349 3.7 14.4 1.0
N A:CYS323 3.9 15.2 1.0
CA A:HIS349 4.1 13.8 1.0
N A:CYS320 4.1 16.5 1.0
CA A:CYS320 4.2 13.5 1.0
CA A:CYS323 4.2 14.9 1.0
NE2 A:HIS349 4.3 15.0 1.0
CD2 A:HIS349 4.4 16.5 1.0
O A:HIS349 4.5 12.3 1.0
CA A:CYS318 4.6 17.8 1.0
O A:CYS320 4.6 11.3 1.0
C A:CYS318 4.6 18.6 1.0
C A:CYS320 4.7 11.5 1.0
O A:CYS318 4.7 19.5 1.0
C A:HIS349 4.7 14.3 1.0
CB A:VAL322 4.8 12.6 1.0
C A:VAL322 4.9 14.7 1.0

Reference:

U.Gradler, H.D.Gerber, D.M.Goodenough-Lashua, G.A.Garcia, R.Ficner, K.Reuter, M.T.Stubbs, G.Klebe. A New Target For Shigellosis: Rational Design and Crystallographic Studies of Inhibitors of Trna-Guanine Transglycosylase. J.Mol.Biol. V. 306 455 2001.
ISSN: ISSN 0022-2836
PubMed: 11178905
DOI: 10.1006/JMBI.2000.4256
Page generated: Sun Oct 13 00:21:47 2024

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