Chlorine in PDB 3cwl: Crystal Structure of Alpha-1-Antitrypsin, Crystal Form B

The structure of Crystal Structure of Alpha-1-Antitrypsin, Crystal Form B, PDB code: 3cwl was solved by C.J.Morton, G.Hansen, S.C.Feil, J.J.Adams, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.13 / 2.44
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.225, 51.898, 206.684, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 26.4

The binding sites of Chlorine atom in the Crystal Structure of Alpha-1-Antitrypsin, Crystal Form B (pdb code 3cwl). 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 Alpha-1-Antitrypsin, Crystal Form B, PDB code: 3cwl:

Chlorine binding site 1 out of 1 in the Crystal Structure of Alpha-1-Antitrypsin, Crystal Form B


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 Alpha-1-Antitrypsin, Crystal Form B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl395 b:21.6 occ:1.00 O A:HOH445 2.8 22.6 1.0 O A:HOH425 3.0 9.5 1.0 O A:HOH399 3.2 18.2 1.0 N A:LYS243 3.2 16.2 1.0 NH2 A:ARG281 3.3 19.1 1.0 CB A:LYS243 3.8 16.6 1.0 CA A:MET242 3.9 14.8 1.0 NH1 A:ARG281 4.0 20.5 1.0 O A:HOH416 4.0 7.2 1.0 CA A:LYS243 4.1 16.5 1.0 C A:MET242 4.1 15.1 1.0 CZ A:ARG281 4.1 20.8 1.0 CG A:ARG196 4.2 12.4 1.0 CG A:LYS243 4.2 18.0 1.0 CD A:ARG196 4.3 11.5 1.0 O A:LYS243 4.4 16.9 1.0 CD A:LYS243 4.5 19.0 1.0 NE A:ARG196 4.5 9.4 1.0 CB A:MET242 4.5 14.4 1.0 O A:LEU241 4.6 12.7 1.0 CB A:GLU195 4.7 16.1 1.0 CB A:ARG196 4.7 14.2 1.0 C A:LYS243 4.8 16.6 1.0 N A:ARG196 4.9 15.3 1.0 CG A:MET242 4.9 14.8 1.0

M.C.Pearce, C.J.Morton, S.C.Feil, G.Hansen, J.J.Adams, M.W.Parker, S.P.Bottomley. Preventing Serpin Aggregation: the Molecular Mechanism of Citrate Action Upon Antitrypsin Unfolding. Protein Sci. V. 17 2127 2008.
ISSN: ISSN 0961-8368
PubMed: 18780818
DOI: 10.1110/PS.037234.108