Chlorine in PDB 3uvi: Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant

All present enzymatic activity of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant:
2.4.2.29;

The structure of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant, PDB code: 3uvi 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)	35.08 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.019, 64.984, 70.488, 90.00, 95.60, 90.00
R / Rfree (%)	16.5 / 19.1

The structure of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant also contains other interesting chemical elements:

Iodine	(I)	10 atoms
Zinc	(Zn)	1 atom

The binding sites of Chlorine atom in the Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant (pdb code 3uvi). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant, PDB code: 3uvi:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Trna-Guanine Transglycosylase C158S C281S W326E E339Q 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 C158S C281S W326E E339Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl396 b:26.4 occ:1.00 O A:HOH449 3.1 16.5 1.0 O A:HOH423 3.7 32.9 1.0 CB A:ARG77 4.0 21.9 1.0 CA A:PRO78 4.0 17.4 1.0 CB A:PRO78 4.2 17.9 1.0 CD A:ARG77 4.3 37.4 1.0 CG A:ARG77 4.4 30.0 1.0 CA A:ARG77 4.5 17.4 1.0 N A:PRO78 4.5 11.9 1.0 C A:ARG77 4.7 12.9 1.0

Chlorine binding site 2 out of 2 in the Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl397 b:41.5 occ:1.00 O A:HOH657 2.5 39.2 1.0 O A:HOH618 2.9 45.2 1.0 N A:THR164 3.1 21.9 1.0 CD A:ARG167 3.3 24.9 0.6 CA A:ALA163 3.5 20.0 1.0 CG2 A:THR164 3.7 23.3 1.0 CB A:ARG167 3.8 17.2 0.4 OG1 A:THR164 3.8 20.6 1.0 C A:ALA163 3.8 19.8 1.0 CG A:ARG167 3.9 22.6 0.6 CB A:ARG167 3.9 17.4 0.6 O A:PRO162 3.9 25.3 1.0 CG A:ARG167 3.9 22.1 0.4 CB A:THR164 4.1 20.6 1.0 NE A:ARG167 4.2 33.9 0.6 CA A:THR164 4.2 22.8 1.0 NH1 A:ARG167 4.2 34.4 0.6 CB A:ALA163 4.2 24.2 1.0 CD A:ARG167 4.5 26.4 0.4 CZ A:ARG167 4.5 27.7 0.6 N A:ALA163 4.6 26.0 1.0 C A:PRO162 4.6 25.5 1.0 O A:THR164 5.0 19.2 1.0 NE A:ARG167 5.0 32.9 0.4

S.Jakobi, T.X.Nguyen, F.Debaene, A.Metz, S.Sanglier-Cianferani, K.Reuter, G.Klebe. Hot-Spot Analysis to Dissect the Functional Protein-Protein Interface of A Trna-Modifying Enzyme. Proteins V. 82 2713 2014.
ISSN: ISSN 0887-3585
PubMed: 24975703
DOI: 10.1002/PROT.24637