Sodium 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:

Chlorine

(Cl)

2 atoms

The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Serine Hydrolase CCSP0084 From the Polyaromatic Hydrocarbon (Pah)-Degrading Bacterium Cycloclasticus Zankles, PDB code: 4i3f:

Sodium binding site 1 out of 1 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 Sodium with other atoms in the Na 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:Na303 b:47.4 occ:1.00 OE2 A:GLU119 2.3 43.7 1.0 ND1 A:HIS117 2.5 22.7 1.0 O A:HOH762 2.7 44.2 1.0 O A:HOH494 2.8 30.1 1.0 O A:HOH557 3.1 27.3 0.5 CE1 A:HIS117 3.5 21.4 1.0 CD A:GLU119 3.5 32.0 1.0 CG A:HIS117 3.5 15.9 1.0 O A:HOH571 3.6 41.0 1.0 CB A:HIS117 3.7 15.3 1.0 OE1 A:GLU119 3.9 28.2 1.0 CA A:HIS117 3.9 13.7 1.0 O A:ARG116 4.2 16.1 1.0 O A:HOH669 4.3 52.0 1.0 O A:HOH557 4.5 21.1 0.5 NE2 A:HIS117 4.6 18.9 1.0 CD2 A:HIS117 4.6 14.7 1.0 CG A:GLU119 4.7 30.2 1.0 C A:HIS117 4.8 15.8 1.0 N A:HIS117 4.9 16.7 1.0 CG A:ARG120 4.9 12.2 1.0 C A:ARG116 5.0 14.4 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