Chlorine in PDB 4i3f: Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles

The structure of Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles, PDB code: 4i3f was solved by P.J.Stogios, X.Xu, A.Dong, H.Cui, M.Alcaide, J.Tornes, C.Gertler, M.M.Yakimov, P.N.Golyshin, M.Ferrer, A.Savchenko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.61 / 1.69
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	81.543, 49.691, 67.995, 90.00, 105.89, 90.00
R / Rfree (%)	14.6 / 18.7

The structure of Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles (pdb code 4i3f). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles, PDB code: 4i3f:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles


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 Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:22.8 occ:1.00 O A:HOH680 2.9 69.5 1.0 O A:HOH682 3.0 23.4 1.0 O A:HOH739 3.1 40.4 1.0 ND2 A:ASN41 3.3 18.2 1.0 N A:GLY33 3.4 18.9 1.0 C A:GLY31 3.6 17.1 1.0 NE1 A:TRP259 3.6 24.1 1.0 CA A:GLY31 3.7 14.8 1.0 CB A:ALA36 3.8 19.7 1.0 N A:SER32 3.8 14.6 1.0 OD1 A:ASN41 3.8 15.3 1.0 N A:GLY31 4.0 10.6 1.0 CG A:ASN41 4.0 19.4 1.0 O A:GLY31 4.0 15.1 1.0 CA A:GLY33 4.0 22.9 1.0 ND2 A:ASN103 4.2 18.5 1.0 CZ2 A:TRP259 4.2 24.6 1.0 CE2 A:TRP259 4.3 20.3 1.0 C A:SER32 4.4 17.6 1.0 CA A:SER32 4.6 11.9 1.0 CA A:ALA36 4.7 17.3 1.0 CD1 A:TRP259 4.8 23.1 1.0 O A:GLY33 4.9 19.7 1.0 O A:HOH733 4.9 50.9 1.0 C A:GLY33 5.0 25.2 1.0 CL A:CL302 5.0 37.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:37.5 occ:1.00 OG A:SER104 3.1 31.9 1.0 OG A:SER32 3.1 22.1 1.0 O A:HOH682 3.3 23.4 1.0 N A:SER32 3.3 14.6 1.0 O A:HOH653 3.6 33.8 1.0 CB A:SER104 3.7 21.1 1.0 C A:SER32 3.7 17.6 1.0 CA A:SER32 3.8 11.9 1.0 N A:GLY33 3.8 18.9 1.0 CB A:SER32 4.1 18.9 1.0 NE2 A:HIS258 4.2 18.2 1.0 O A:SER32 4.2 19.9 1.0 CE1 A:PHE162 4.3 22.6 1.0 C A:GLY31 4.4 17.1 1.0 CZ A:PHE162 4.5 20.3 1.0 CD2 A:HIS258 4.5 15.9 1.0 CD1 A:LEU140 4.6 16.3 1.0 CA A:GLY31 4.6 14.8 1.0 CA A:GLY33 4.7 22.9 1.0 NE1 A:TRP144 4.7 16.1 1.0 CL A:CL301 5.0 22.8 1.0

M.Alcaide, J.Tornes, P.J.Stogios, X.Xu, C.Gertler, R.Di Leo, R.Bargiela, A.Lafraya, M.E.Guazzaroni, N.Lopez-Cortes, T.N.Chernikova, O.V.Golyshina, T.Y.Nechitaylo, I.Plumeier, D.H.Pieper, M.M.Yakimov, A.Savchenko, P.N.Golyshin, M.Ferrer. Single Residues Dictate the Co-Evolution of Dual Esterases: Mcp Hydrolases From the Alpha / Beta Hydrolase Family. Biochem.J. V. 454 157 2013.
ISSN: ISSN 0264-6021
PubMed: 23750508
DOI: 10.1042/BJ20130552