Chlorine in PDB 8aqr: Native Crystal Structure of the N-Terminal Beta-Hairpin Docking (Bhd) Domain of the Aerj Halogenase, From the Aeruginosin Biosynthetic Assembly Line

The structure of Native Crystal Structure of the N-Terminal Beta-Hairpin Docking (Bhd) Domain of the Aerj Halogenase, From the Aeruginosin Biosynthetic Assembly Line, PDB code: 8aqr was solved by C.D.Fage, J.R.Lewandowski, G.L.Challis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.28 / 1.46
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.532, 57.391, 62.168, 90, 99.68, 90
R / Rfree (%)	19.6 / 23.5

The binding sites of Chlorine atom in the Native Crystal Structure of the N-Terminal Beta-Hairpin Docking (Bhd) Domain of the Aerj Halogenase, From the Aeruginosin Biosynthetic Assembly Line (pdb code 8aqr). 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 Native Crystal Structure of the N-Terminal Beta-Hairpin Docking (Bhd) Domain of the Aerj Halogenase, From the Aeruginosin Biosynthetic Assembly Line, PDB code: 8aqr:

Chlorine binding site 1 out of 1 in the Native Crystal Structure of the N-Terminal Beta-Hairpin Docking (Bhd) Domain of the Aerj Halogenase, From the Aeruginosin Biosynthetic Assembly Line


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Native Crystal Structure of the N-Terminal Beta-Hairpin Docking (Bhd) Domain of the Aerj Halogenase, From the Aeruginosin Biosynthetic Assembly Line within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl101 b:59.7 occ:1.00 O B:HOH225 3.6 49.3 1.0 CD B:LYS4 4.1 45.8 1.0 NZ B:LYS4 4.3 64.7 1.0 OE2 B:GLU45 4.8 55.8 1.0 CE B:LYS4 4.8 48.2 1.0

M.J.Beech, C.D.Fage, H.G.Smith, S.Kosol, A.Gallo, D.Bahia, M.Jenner, J.R.Lewandowski, G.L.Challis. Tandem Halogenation and Condensation in Aeruginosin Biosynthesis Is Directed By Docking Domain-Mediated Carrier Protein Recruitment To Be Published.