Chlorine in PDB 4h2w: Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Amp

The structure of Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Amp, PDB code: 4h2w was solved by M.Luic, I.Weygand-Durasevic, N.Ivic, M.Mocibob, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.76 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	99.695, 101.248, 102.997, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 19.6

The structure of Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Amp also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Amp (pdb code 4h2w). 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 Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Amp, PDB code: 4h2w:

Chlorine binding site 1 out of 1 in the Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Amp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Engineered Bradyrhizobium Japonicum Glycine:[Carrier Protein] Ligase Complexed with Carrier Protein From Agrobacterium Tumefaciens and Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:25.4 occ:1.00 N3 A:5GP403 2.8 22.8 0.7 N A:ARG286 3.2 10.0 1.0 N A:ASP285 3.2 9.4 1.0 C A:GLY283 3.3 12.7 1.0 CA A:GLY283 3.3 9.9 1.0 N2 A:5GP403 3.4 19.1 0.7 C2 A:5GP403 3.5 20.2 0.7 N A:MET284 3.5 10.0 1.0 CB A:ASP285 3.7 10.7 1.0 O A:GLY283 3.7 10.1 1.0 O A:ARG173 3.8 11.3 1.0 C4 A:5GP403 3.8 22.8 0.7 CA A:ASP285 3.8 10.8 1.0 C1' A:5GP403 3.8 21.6 0.7 CB A:PHE172 3.9 10.4 1.0 CD2 A:PHE172 3.9 14.7 1.0 C A:ASP285 4.0 14.0 1.0 CB A:ARG286 4.1 13.0 1.0 CG A:ARG286 4.1 15.0 1.0 N9 A:5GP403 4.2 23.8 0.7 C A:MET284 4.2 13.2 1.0 CG A:PHE172 4.2 13.9 1.0 CA A:ARG286 4.3 9.6 1.0 CA A:MET284 4.4 9.1 1.0 SD A:MET174 4.5 14.2 0.5 O2' A:5GP403 4.5 25.9 0.7 OD2 A:ASP285 4.5 16.8 1.0 CD A:ARG286 4.6 18.1 1.0 O4' A:5GP403 4.6 30.1 0.7 CG A:ASP285 4.6 20.3 1.0 N A:ARG173 4.7 12.3 1.0 C2' A:5GP403 4.7 23.0 0.7 N1 A:5GP403 4.8 11.4 0.7 C A:ARG173 4.8 12.5 1.0 N A:GLY283 4.8 9.9 1.0 CE2 A:PHE172 4.9 19.3 1.0 CA A:PHE172 5.0 12.6 1.0

M.Mocibob, N.Ivic, M.Luic, I.Weygand-Durasevic. Adaptation of Aminoacyl-Trna Synthetase Catalytic Core to Carrier Protein Aminoacylation. Structure V. 21 614 2013.
ISSN: ISSN 0969-2126
PubMed: 23541895
DOI: 10.1016/J.STR.2013.02.017