Chlorine in PDB 5om8: Crystal Form 2 of ALPHA1-Antichymotrypsin Variant Dbs-II-Allo: An Allosterically Modulated Drug-Binding Serpin For Doxorubicin

The structure of Crystal Form 2 of ALPHA1-Antichymotrypsin Variant Dbs-II-Allo: An Allosterically Modulated Drug-Binding Serpin For Doxorubicin, PDB code: 5om8 was solved by K.Schmidt, Y.A.Muller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.58 / 2.20
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.542, 84.542, 97.519, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 24.2

The structure of Crystal Form 2 of ALPHA1-Antichymotrypsin Variant Dbs-II-Allo: An Allosterically Modulated Drug-Binding Serpin For Doxorubicin also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Chlorine atom in the Crystal Form 2 of ALPHA1-Antichymotrypsin Variant Dbs-II-Allo: An Allosterically Modulated Drug-Binding Serpin For Doxorubicin (pdb code 5om8). 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 Form 2 of ALPHA1-Antichymotrypsin Variant Dbs-II-Allo: An Allosterically Modulated Drug-Binding Serpin For Doxorubicin, PDB code: 5om8:

Chlorine binding site 1 out of 1 in the Crystal Form 2 of ALPHA1-Antichymotrypsin Variant Dbs-II-Allo: An Allosterically Modulated Drug-Binding Serpin For Doxorubicin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Form 2 of ALPHA1-Antichymotrypsin Variant Dbs-II-Allo: An Allosterically Modulated Drug-Binding Serpin For Doxorubicin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:32.8 occ:1.00 NE A:ARG349 3.0 38.3 1.0 OG B:SER392 3.2 26.7 1.0 NH2 A:ARG349 3.3 33.6 1.0 CZ A:ARG349 3.5 38.7 1.0 O B:MET378 3.6 25.7 1.0 CD1 B:ILE380 3.6 37.9 1.0 N B:MET391 3.6 23.6 1.0 CA B:MET391 3.7 23.5 1.0 N B:SER392 3.7 21.1 1.0 C B:MET391 3.7 22.6 1.0 CB B:PHE390 3.7 23.6 1.0 C B:PHE390 3.8 23.4 1.0 CB B:MET378 3.8 24.8 1.0 C B:MET378 3.8 26.1 1.0 CB B:SER392 3.8 29.2 1.0 O B:PHE390 3.9 24.1 1.0 CD A:ARG349 4.0 31.0 1.0 CD1 A:ILE51 4.2 26.9 1.0 N B:ILE379 4.3 27.5 1.0 O B:MET391 4.4 23.7 1.0 CA B:PHE390 4.4 25.0 1.0 CA B:SER392 4.4 22.4 1.0 CA B:MET378 4.5 26.4 1.0 CA B:ILE379 4.6 27.1 1.0 N B:ILE380 4.8 34.4 1.0 CG A:ARG349 4.8 28.4 1.0 C B:ILE379 4.8 30.1 1.0 NH1 A:ARG349 4.8 35.4 1.0 CG1 B:ILE380 4.8 34.7 1.0 CG B:PHE390 4.9 25.1 1.0

K.Schmidt, B.R.Gardill, A.Kern, P.Kirchweger, M.Borsch, Y.A.Muller. Design of An Allosterically Modulated Doxycycline and Doxorubicin Drug-Binding Protein. Proc. Natl. Acad. Sci. V. 115 5744 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29760101
DOI: 10.1073/PNAS.1716666115