Sodium in PDB 6jjq: Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution.

All present enzymatic activity of Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution.:
3.1.1.29;

The structure of Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution., PDB code: 6jjq was solved by V.Viswanathan, H.R.Bairagya, P.Sharma, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.83 / 0.99
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.139, 65.976, 76.011, 90.00, 90.00, 90.00
R / Rfree (%)	13 / 13.9

The structure of Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution. also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Sodium atom in the Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution. (pdb code 6jjq). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution., PDB code: 6jjq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Na205 b:13.4 occ:0.90 H A:ALA153 1.9 9.3 1.0 HH2 A:TRP27 2.8 9.8 1.0 O A:GLN19 2.8 10.6 1.0 N A:ALA153 2.9 8.7 1.0 OE1 A:GLN158 2.9 10.2 1.0 HA A:LYS152 2.9 9.3 1.0 HB3 A:ALA153 3.0 9.3 1.0 HB2 A:ALA153 3.1 9.3 1.0 HZ2 A:TRP27 3.3 9.8 1.0 HE1 A:MET161 3.4 10.9 1.0 HG3 A:ARG21 3.4 9.2 1.0 CB A:ALA153 3.4 9.1 1.0 HG2 A:ARG21 3.5 9.2 1.0 CH2 A:TRP27 3.5 10.6 1.0 HA A:ARG21 3.6 8.5 1.0 HA A:THR20 3.7 9.2 1.0 HG3 A:LYS152 3.7 15.4 1.0 CA A:LYS152 3.7 9.6 1.0 CZ2 A:TRP27 3.7 10.0 1.0 N A:ARG21 3.7 8.4 1.0 CA A:ALA153 3.7 8.4 1.0 C A:LYS152 3.8 9.2 1.0 H A:ARG21 3.8 9.2 1.0 O A:HOH364 3.9 12.1 1.0 C A:GLN19 3.9 9.7 1.0 CG A:ARG21 3.9 9.5 1.0 C A:THR20 3.9 8.2 1.0 O A:GLY151 4.0 10.8 1.0 CD A:GLN158 4.1 9.0 1.0 CA A:ARG21 4.1 8.1 1.0 HE3 A:MET161 4.2 10.9 1.0 CE A:MET161 4.2 10.8 1.0 CA A:THR20 4.2 9.2 1.0 HB1 A:ALA153 4.3 9.3 1.0 CG A:LYS152 4.4 11.0 1.0 HE21 A:GLN158 4.4 10.1 1.0 HG2 A:LYS152 4.4 15.4 1.0 HA A:ALA153 4.4 9.4 1.0 O A:THR20 4.4 8.4 1.0 N A:THR20 4.5 9.3 1.0 CB A:LYS152 4.6 10.0 1.0 HE2 A:MET161 4.6 10.9 1.0 CB A:ARG21 4.6 8.8 1.0 NE2 A:GLN158 4.6 10.1 1.0 O A:ALA153 4.7 9.4 1.0 CZ3 A:TRP27 4.7 9.8 1.0 C A:ALA153 4.7 9.2 1.0 HB3 A:GLN19 4.7 16.5 1.0 N A:LYS152 4.8 9.7 1.0 HB2 A:GLN158 4.8 9.1 1.0 C A:GLY151 4.8 10.2 1.0 HB2 A:LYS152 4.9 10.7 1.0 HZ1 A:LYS152 4.9 17.6 1.0 HZ3 A:TRP27 4.9 9.8 1.0 O A:LYS152 5.0 9.8 1.0 HA A:GLN19 5.0 10.2 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Na206 b:14.4 occ:0.85 H A:GLN182 2.2 10.2 1.0 HD2 A:PRO181 2.8 11.8 1.0 HB3 A:GLN179 2.8 10.0 1.0 HA A:GLN179 2.9 9.9 1.0 HB2 A:GLN182 2.9 11.1 1.0 N A:GLN182 3.1 10.0 1.0 HB2 A:PRO181 3.1 13.4 1.0 HB3 A:GLN182 3.2 11.1 1.0 CA A:GLN179 3.4 9.7 1.0 CB A:GLN182 3.4 10.6 1.0 CB A:GLN179 3.4 9.9 1.0 C A:GLN179 3.5 9.7 1.0 HG2 A:GLN179 3.5 10.1 1.0 CD A:PRO181 3.6 12.2 1.0 O A:GLN179 3.7 10.3 1.0 N A:PRO181 3.8 10.8 1.0 HE22 A:GLN182 3.8 11.3 1.0 CB A:PRO181 3.8 13.2 1.0 CA A:GLN182 3.8 10.2 1.0 CG A:GLN179 4.0 9.8 1.0 HE22 A:GLN179 4.0 11.5 1.0 HG2 A:PRO181 4.0 14.3 1.0 C A:PRO181 4.0 10.5 1.0 CG A:PRO181 4.1 14.0 1.0 N A:VAL180 4.1 11.5 1.0 CA A:PRO181 4.1 10.7 1.0 HB2 A:GLN179 4.3 10.0 1.0 H A:ALA183 4.3 9.8 1.0 H A:VAL180 4.3 16.1 1.0 HD3 A:PRO181 4.3 11.8 1.0 HA A:GLN182 4.4 10.2 1.0 NE2 A:GLN182 4.5 12.9 1.0 C A:VAL180 4.6 10.9 1.0 HB3 A:PRO181 4.7 13.4 1.0 HG3 A:GLN179 4.7 10.1 1.0 NE2 A:GLN179 4.7 11.6 1.0 N A:GLN179 4.8 9.5 1.0 CG A:GLN182 4.8 11.7 1.0 CD A:GLN179 4.9 11.0 1.0 CA A:VAL180 5.0 11.5 1.0 HE21 A:GLN182 5.0 11.3 1.0

V.Viswanathan, H.R.Bairagya, P.Sharma, S.Sharma, T.P.Singh. Crystal Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii at 0.99 A Resolution. To Be Published.