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Chlorine in PDB 4dy1: Trna-Guanine Transglycosylase F92C C158S C281S Mutant

Enzymatic activity of Trna-Guanine Transglycosylase F92C C158S C281S Mutant

All present enzymatic activity of Trna-Guanine Transglycosylase F92C C158S C281S Mutant:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase F92C C158S C281S Mutant, PDB code: 4dy1 was solved by S.Jakobi, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.16 / 2.05
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.828, 64.601, 71.092, 90.00, 96.39, 90.00
R / Rfree (%) 16.6 / 22

Other elements in 4dy1:

The structure of Trna-Guanine Transglycosylase F92C C158S C281S Mutant also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Trna-Guanine Transglycosylase F92C C158S C281S Mutant (pdb code 4dy1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Trna-Guanine Transglycosylase F92C C158S C281S Mutant, PDB code: 4dy1:

Chlorine binding site 1 out of 1 in 4dy1

Go back to Chlorine Binding Sites List in 4dy1
Chlorine binding site 1 out of 1 in the Trna-Guanine Transglycosylase F92C C158S C281S Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Trna-Guanine Transglycosylase F92C C158S C281S Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:29.9
occ:1.00
ZN A:ZN402 2.2 28.5 1.0
NZ A:LYS52 2.8 31.2 1.0
CG2 A:THR47 3.3 31.8 1.0
NE2 A:HIS73 3.6 28.7 1.0
CD2 A:HIS73 3.9 23.8 1.0
CB A:THR47 4.0 38.0 1.0
CE A:MET93 4.0 32.6 0.9
CE A:LYS52 4.1 26.6 1.0
CD2 A:LEU74 4.2 17.6 1.0
CA A:THR47 4.2 26.6 1.0
CD A:LYS52 4.3 29.9 1.0
O A:GLY46 4.7 28.1 1.0
CE1 A:HIS73 4.9 29.4 1.0

Reference:

S.Jakobi, P.T.Nguyen, F.Debaene, S.Cianferani, K.Reuter, G.Klebe. What Glues A Homodimer Together: Systematic Analysis of the Stabilizing Effect of An Aromatic Hot Spot in the Protein-Protein Interface of the Trna-Modifying Enzyme Tgt. Acs Chem.Biol. V. 10 1897 2015.
ISSN: ISSN 1554-8929
PubMed: 25951081
DOI: 10.1021/ACSCHEMBIO.5B00028
Page generated: Sat Dec 12 10:33:07 2020

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