Chlorine in PDB 4jg3: Crystal Structure of Catabolite Repression Control Protein (Crc) From Pseudomonas Aeruginosa

The structure of Crystal Structure of Catabolite Repression Control Protein (Crc) From Pseudomonas Aeruginosa, PDB code: 4jg3 was solved by I.Grishkovskaya, T.Milojevic, E.Sonnleitner, U.Blaesi, K.Djinovic-Carugo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.59 / 1.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.659, 74.659, 123.161, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 22

The binding sites of Chlorine atom in the Crystal Structure of Catabolite Repression Control Protein (Crc) From Pseudomonas Aeruginosa (pdb code 4jg3). 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 Catabolite Repression Control Protein (Crc) From Pseudomonas Aeruginosa, PDB code: 4jg3:

Chlorine binding site 1 out of 1 in the Crystal Structure of Catabolite Repression Control Protein (Crc) From Pseudomonas Aeruginosa


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 Catabolite Repression Control Protein (Crc) From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:82.3 occ:1.00 OD1 A:ASP130 3.1 47.1 1.0 O A:HOH423 3.2 44.1 1.0 CE A:MET129 3.8 38.1 1.0 CG A:ASP130 3.9 44.0 1.0 OD2 A:ASP130 4.1 53.5 1.0 O A:PHE126 4.3 35.7 1.0 O A:PRO176 4.3 38.9 1.0 CG A:PHE126 4.4 42.5 1.0 CB A:MET129 4.5 35.2 1.0 CB A:PHE126 4.5 42.7 1.0 O A:HOH443 4.6 40.3 1.0 CA A:PHE126 4.7 40.6 1.0 CD1 A:PHE126 4.7 44.4 1.0 CB A:PRO176 4.7 44.9 1.0 SD A:MET129 4.8 37.4 1.0 CD2 A:PHE126 4.8 53.5 1.0 CB A:TRP180 4.9 34.2 1.0 C A:PHE126 4.9 35.7 1.0 C A:PRO176 5.0 35.1 1.0

T.Milojevic, I.Grishkovskaya, E.Sonnleitner, K.Djinovic-Carugo, U.Blasi. The Pseudomonas Aeruginosa Catabolite Repression Control Protein Crc Is Devoid of Rna Binding Activity Plos One V. 8 64609 2013.
ISSN: ESSN 1932-6203
PubMed: 23717639
DOI: 10.1371/JOURNAL.PONE.0064609