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Zinc in PDB 4fsa: Trna-Guanine Transglycosylase Soaked with Pyridyl-Alkine-Substituted Lin-Benzoguanine Ligand

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

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

Protein crystallography data

The structure of Trna-Guanine Transglycosylase Soaked with Pyridyl-Alkine-Substituted Lin-Benzoguanine Ligand, PDB code: 4fsa 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) 50.00 / 1.62
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.079, 64.901, 70.784, 90.00, 96.33, 90.00
R / Rfree (%) 17.2 / 20.7

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 4fsa

Go back to Zinc Binding Sites List in 4fsa
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase Soaked with Pyridyl-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 Soaked with Pyridyl-Alkine-Substituted Lin-Benzoguanine Ligand within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:16.2
occ:1.00
 ND1 A:HIS349 2.2 14.5 1.0
SG A:CYS320 2.3 15.5 1.0
SG A:CYS323 2.3 16.1 1.0
SG A:CYS318 2.3 17.8 1.0
CE1 A:HIS349 3.0 17.7 1.0
CB A:CYS318 3.2 18.8 1.0
CB A:CYS323 3.3 12.9 1.0
CG A:HIS349 3.3 12.9 1.0
CB A:CYS320 3.4 15.9 1.0
CB A:HIS349 3.8 11.4 1.0
N A:CYS323 3.9 15.3 1.0
N A:CYS320 4.1 17.9 1.0
CA A:HIS349 4.2 11.8 1.0
NE2 A:HIS349 4.2 15.4 1.0
CA A:CYS320 4.2 17.9 1.0
CA A:CYS323 4.2 16.2 1.0
CD2 A:HIS349 4.4 13.6 1.0
CA A:CYS318 4.5 19.1 1.0
O A:HIS349 4.6 13.4 1.0
O A:CYS320 4.7 15.1 1.0
C A:CYS320 4.7 15.5 1.0
C A:CYS318 4.7 21.2 1.0
CB A:VAL322 4.8 17.4 1.0
C A:HIS349 4.8 13.4 1.0
O A:CYS318 4.9 23.4 1.0
C A:VAL322 4.9 16.4 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 22:52:34 2024

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