Chlorine in PDB 3cjt: Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11

The structure of Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11, PDB code: 3cjt was solved by H.Demirci, S.T.Gregory, A.E.Dahlberg, G.Jogl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.74 / 2.30
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.822, 69.943, 379.007, 90.00, 90.47, 90.00
R / Rfree (%)	19.4 / 25.9

The binding sites of Chlorine atom in the Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11 (pdb code 3cjt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11, PDB code: 3cjt:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl256 b:47.0 occ:1.00 NH2 A:ARG170 3.2 29.8 1.0 NE E:ARG170 3.5 34.4 1.0 O E:HOH265 3.7 44.8 1.0 O A:HOH519 3.8 31.9 1.0 CD E:ARG170 3.8 33.8 1.0 CB E:PHE182 4.1 23.8 1.0 CD2 E:PHE182 4.2 24.8 1.0 NZ E:LYS123 4.2 28.7 1.0 CB E:LEU146 4.3 23.7 1.0 CZ A:ARG170 4.4 30.1 1.0 CB E:ARG170 4.4 30.3 1.0 CG E:PHE182 4.5 24.0 1.0 O E:PHE182 4.5 22.8 1.0 CZ E:ARG170 4.5 34.7 1.0 CD2 E:LEU146 4.7 24.8 1.0 NE A:ARG170 4.7 30.9 1.0 NH2 E:ARG170 4.8 35.8 1.0 CG E:ARG170 4.8 32.0 1.0 CG E:LEU146 5.0 25.4 1.0

Chlorine binding site 2 out of 4 in the Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl257 b:47.2 occ:1.00 NH2 E:ARG170 2.9 35.8 1.0 NE A:ARG170 3.5 30.9 1.0 O A:HOH310 3.6 32.8 1.0 CD A:ARG170 3.8 30.8 1.0 O E:HOH445 3.8 33.4 1.0 CB A:PHE182 4.0 21.9 1.0 CD2 A:PHE182 4.1 23.1 1.0 NZ A:LYS123 4.1 31.9 1.0 CZ E:ARG170 4.2 34.7 1.0 CB A:LEU146 4.3 24.0 1.0 CG A:PHE182 4.4 22.9 1.0 CB A:ARG170 4.4 29.1 1.0 O A:PHE182 4.6 20.3 1.0 CZ A:ARG170 4.6 30.1 1.0 NE E:ARG170 4.6 34.4 1.0 CD2 A:LEU146 4.7 23.4 1.0 CG A:ARG170 4.8 29.5 1.0 NH2 A:ARG170 4.9 29.8 1.0 O A:ALA145 5.0 23.5 1.0 CG A:LEU146 5.0 24.6 1.0 CA A:PHE182 5.0 22.9 1.0

Chlorine binding site 3 out of 4 in the Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11 within 5.0Å range: probe atom residue distance (Å) B Occ I:Cl257 b:53.8 occ:1.00 O M:HOH305 3.4 35.7 1.0 NH2 I:ARG170 3.4 39.4 1.0 NH1 I:ARG170 3.6 44.3 1.0 NE M:ARG170 3.7 32.7 1.0 O I:HOH276 3.8 43.4 1.0 CB M:PHE182 4.0 27.3 1.0 CZ I:ARG170 4.0 38.8 1.0 CD M:ARG170 4.1 33.5 1.0 NZ M:LYS123 4.2 29.2 1.0 CB M:LEU146 4.2 28.2 1.0 CD2 M:PHE182 4.3 27.4 1.0 CD2 M:LEU146 4.4 28.0 1.0 O M:PHE182 4.4 24.8 1.0 CG M:PHE182 4.5 28.0 1.0 CB M:ARG170 4.5 32.6 1.0 CZ M:ARG170 4.7 33.9 1.0 CG M:LEU146 4.8 29.1 1.0 NH2 M:ARG170 4.8 32.5 1.0 O M:ALA145 4.9 29.7 1.0 CA M:PHE182 4.9 27.2 1.0 CG M:ARG170 5.0 33.4 1.0 CA M:LEU146 5.0 28.9 1.0

Chlorine binding site 4 out of 4 in the Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Ribosomal Protein L11 Methyltransferase (Prma) in Complex with Dimethylated Ribosomal Protein L11 within 5.0Å range: probe atom residue distance (Å) B Occ I:Cl258 b:48.2 occ:1.00 NH1 I:ARG170 2.8 44.3 1.0 NH2 M:ARG170 2.9 32.5 1.0 O M:HOH280 3.8 37.0 1.0 O I:HOH369 3.9 42.0 1.0 CZ I:ARG170 3.9 38.8 1.0 CD I:ARG170 4.0 34.1 1.0 CZ M:ARG170 4.1 33.9 1.0 CB I:PHE182 4.2 28.6 1.0 NZ I:LYS123 4.2 33.4 1.0 CD2 I:PHE182 4.3 28.9 1.0 NE I:ARG170 4.4 37.3 1.0 CB I:ARG170 4.4 32.2 1.0 CB I:LEU146 4.5 29.5 1.0 CG I:PHE182 4.6 29.6 1.0 O I:PHE182 4.6 26.4 1.0 NE M:ARG170 4.6 32.7 1.0 CG I:ARG170 4.8 33.6 1.0 CD2 I:LEU146 4.8 28.9 1.0 NH2 I:ARG170 5.0 39.4 1.0

H.Demirci, S.T.Gregory, A.E.Dahlberg, G.Jogl. Multiple-Site Trimethylation of Ribosomal Protein L11 By the Prma Methyltransferase. Structure V. 16 1059 2008.
ISSN: ISSN 0969-2126
PubMed: 18611379
DOI: 10.1016/J.STR.2008.03.016