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Zinc in PDB 4fr1: Trna-Guanine Transglycosylase Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand

Enzymatic activity of Trna-Guanine Transglycosylase Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand

All present enzymatic activity of Trna-Guanine Transglycosylase Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand, PDB code: 4fr1 was solved by F.Immekus, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.74
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 84.818, 64.845, 71.418, 90.00, 93.97, 90.00
R / Rfree (%) 18.5 / 23.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand (pdb code 4fr1). 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 Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand, PDB code: 4fr1:

Zinc binding site 1 out of 1 in 4fr1

Go back to Zinc Binding Sites List in 4fr1
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand


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 Cocrystallized with Alkine-Substituted Lin-Benzoguanine Ligand within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:23.4
occ:1.00
 SG A:CYS323 2.3 23.7 1.0
SG A:CYS318 2.3 27.6 1.0
ND1 A:HIS349 2.3 14.0 1.0
SG A:CYS320 2.3 27.3 1.0
CE1 A:HIS349 3.0 19.2 1.0
CB A:CYS323 3.1 26.6 1.0
CB A:CYS318 3.2 34.8 1.0
CB A:CYS320 3.2 38.0 1.0
CG A:HIS349 3.5 10.9 1.0
N A:CYS323 3.9 29.5 1.0
CB A:HIS349 3.9 14.6 1.0
N A:CYS320 4.0 31.3 1.0
CA A:CYS323 4.1 26.6 1.0
CA A:CYS320 4.1 31.5 1.0
NE2 A:HIS349 4.2 15.2 1.0
CA A:HIS349 4.3 11.7 1.0
CD2 A:HIS349 4.5 15.0 1.0
CA A:CYS318 4.5 34.9 1.0
C A:CYS320 4.6 32.4 1.0
O A:CYS320 4.6 33.9 1.0
O A:HIS349 4.6 15.0 1.0
C A:CYS318 4.7 36.5 1.0
O A:CYS318 4.8 32.9 1.0
CB A:VAL322 4.8 33.2 1.0
C A:HIS349 4.9 10.5 1.0
C A:VAL322 4.9 32.6 1.0
CB A:LEU314 5.0 22.6 1.0

Reference:

F.Immekus, L.J.Barandun, M.Betz, F.Debaene, S.Petiot, S.Sanglier-Cianferani, F.Diederich, G.Klebe. Studies on Tgt Homodimer Interface To Be Published.
Page generated: Sat Oct 26 22:51:29 2024

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