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Zinc in PDB 4ipp: Trna-Guanine-Transglycosylase (Tgt) Mutant V262D Apo-Structure

Enzymatic activity of Trna-Guanine-Transglycosylase (Tgt) Mutant V262D Apo-Structure

All present enzymatic activity of Trna-Guanine-Transglycosylase (Tgt) Mutant V262D Apo-Structure:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine-Transglycosylase (Tgt) Mutant V262D Apo-Structure, PDB code: 4ipp was solved by M.Neeb, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.51 / 1.33
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.047, 65.099, 70.337, 90.00, 96.22, 90.00
R / Rfree (%) 13.3 / 15

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine-Transglycosylase (Tgt) Mutant V262D Apo-Structure (pdb code 4ipp). 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 (Tgt) Mutant V262D Apo-Structure, PDB code: 4ipp:

Zinc binding site 1 out of 1 in 4ipp

Go back to Zinc Binding Sites List in 4ipp
Zinc binding site 1 out of 1 in the Trna-Guanine-Transglycosylase (Tgt) Mutant V262D Apo-Structure


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 (Tgt) Mutant V262D Apo-Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:8.9
occ:1.00
ND1 A:HIS349 2.1 8.3 1.0
SG A:CYS323 2.3 9.4 1.0
SG A:CYS320 2.3 9.1 1.0
SG A:CYS318 2.3 10.3 1.0
CE1 A:HIS349 2.9 9.1 1.0
CG A:HIS349 3.2 7.9 1.0
CB A:CYS323 3.3 9.2 1.0
CB A:CYS318 3.3 10.9 1.0
CB A:CYS320 3.4 9.7 1.0
CB A:HIS349 3.7 8.2 1.0
N A:CYS323 3.9 8.9 1.0
CA A:HIS349 4.1 7.4 1.0
NE2 A:HIS349 4.1 8.5 1.0
N A:CYS320 4.2 10.1 1.0
CA A:CYS323 4.2 9.4 1.0
CA A:CYS320 4.2 10.1 1.0
CD2 A:HIS349 4.3 8.8 1.0
O A:HIS349 4.5 7.8 1.0
CA A:CYS318 4.6 9.8 1.0
O A:CYS320 4.7 10.4 1.0
C A:CYS320 4.7 9.5 1.0
C A:CYS318 4.7 10.9 1.0
CB A:VAL322 4.8 8.7 1.0
C A:HIS349 4.8 7.5 1.0
O A:CYS318 4.8 11.7 1.0
C A:VAL322 4.9 8.9 1.0

Reference:

M.Neeb, L.J.Barandun, C.Hohn, A.Heine, F.Diederich, G.Klebe. Investigating the Advantage of Ligands with Residual Mobility in Binding Mutated Tgt To Be Published.
Page generated: Sun Oct 27 00:50:05 2024

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