Chlorine in PDB 3usp: Crystal Structure of Leut in Heptyl-Beta-D-Selenoglucoside

The structure of Crystal Structure of Leut in Heptyl-Beta-D-Selenoglucoside, PDB code: 3usp was solved by H.Wang, J.Elferich, E.Gouaux, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.56 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	89.697, 86.359, 81.399, 90.00, 96.15, 90.00
R / Rfree (%)	22.3 / 23.2

The structure of Crystal Structure of Leut in Heptyl-Beta-D-Selenoglucoside also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Leut in Heptyl-Beta-D-Selenoglucoside (pdb code 3usp). 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 Leut in Heptyl-Beta-D-Selenoglucoside, PDB code: 3usp:

Chlorine binding site 1 out of 1 in the Crystal Structure of Leut in Heptyl-Beta-D-Selenoglucoside


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 Leut in Heptyl-Beta-D-Selenoglucoside within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl603 b:41.8 occ:1.00 OG A:SER165 3.0 24.2 1.0 NZ A:LYS121 3.3 35.2 1.0 O A:HOH717 3.4 30.3 1.0 CB A:SER165 3.6 26.5 1.0 CD1 A:TYR151 3.8 20.4 1.0 SE A:05L608 3.8 50.0 1.0 C2 A:05L608 4.1 55.9 1.0 CA A:TYR151 4.2 20.5 1.0 CD2 A:PHE167 4.2 26.6 1.0 CB A:PHE167 4.3 26.4 1.0 CE A:LYS121 4.3 36.9 1.0 O A:HOH721 4.4 34.3 1.0 CE1 A:TYR151 4.5 23.0 1.0 CD A:LYS121 4.5 27.6 1.0 CG A:TYR151 4.5 23.4 1.0 CB A:TYR151 4.5 21.3 1.0 C1 A:05L608 4.5 49.5 1.0 O A:HOH797 4.7 45.5 1.0 O A:SER150 4.7 22.0 1.0 CG A:PHE167 4.7 26.1 1.0 N A:TYR151 4.7 23.2 1.0 C4 A:05L608 4.8 55.7 1.0 O5 A:05L608 4.8 50.4 1.0 C3 A:05L608 4.9 57.8 1.0 O2 A:05L608 4.9 64.0 1.0 C A:SER150 5.0 24.9 1.0 O3 A:05L608 5.0 57.0 1.0

H.Wang, J.Elferich, E.Gouaux. Structures of Leut in Bicelles Define Conformation and Substrate Binding in A Membrane-Like Context. Nat.Struct.Mol.Biol. V. 19 212 2012.
ISSN: ISSN 1545-9993
PubMed: 22245965
DOI: 10.1038/NSMB.2215