Chlorine in PDB 3bc8: Crystal Structure of Mouse Selenocysteine Synthase

The structure of Crystal Structure of Mouse Selenocysteine Synthase, PDB code: 3bc8 was solved by O.M.Ganichkin, M.C.Wahl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.65
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	59.172, 138.730, 141.660, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 19.9

The binding sites of Chlorine atom in the Crystal Structure of Mouse Selenocysteine Synthase (pdb code 3bc8). 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 Mouse Selenocysteine Synthase, PDB code: 3bc8:

Chlorine binding site 1 out of 1 in the Crystal Structure of Mouse Selenocysteine Synthase


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 Mouse Selenocysteine Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:16.5 occ:1.00 OG A:SER259 3.0 12.7 1.0 O A:HOH625 3.1 16.6 1.0 NH2 A:ARG341 3.3 12.1 1.0 N A:SER260 3.4 11.1 1.0 N A:LYS261 3.4 12.6 1.0 CE A:LYS342 3.6 13.7 1.0 OG A:SER260 3.6 14.6 1.0 CA A:SER259 3.6 11.8 1.0 NZ A:LYS342 3.6 13.7 1.0 CG A:LYS261 3.6 17.8 1.0 CB A:SER259 3.7 12.2 1.0 C A:SER259 3.8 10.9 1.0 CB A:LYS261 3.9 14.2 1.0 CB A:PRO370 4.0 14.6 1.0 O A:HOH519 4.2 14.4 1.0 CA A:SER260 4.2 12.1 1.0 CA A:LYS261 4.3 13.5 1.0 C A:SER260 4.3 12.0 1.0 O A:HOH581 4.4 15.4 1.0 CG A:LYS342 4.5 12.8 1.0 CZ A:ARG341 4.5 13.4 1.0 CB A:SER260 4.5 12.3 1.0 CD A:LYS342 4.6 12.0 1.0 CD A:LYS261 4.6 25.1 1.0 O A:HOH513 4.6 14.2 1.0 CG A:PRO370 4.7 14.1 1.0 O A:SER259 4.7 10.3 1.0 O A:HOH659 4.8 22.6 1.0 O A:HOH713 4.9 28.1 1.0 NE A:ARG341 5.0 12.4 1.0 N A:SER259 5.0 11.5 1.0

O.M.Ganichkin, X.M.Xu, B.A.Carlson, H.Mix, D.L.Hatfield, V.N.Gladyshev, M.C.Wahl. Structure and Catalytic Mechanism of Eukaryotic Selenocysteine Synthase. J.Biol.Chem. V. 283 5849 2008.
ISSN: ISSN 0021-9258
PubMed: 18093968
DOI: 10.1074/JBC.M709342200