Sodium in PDB 2hds: Ampc Beta-Lactamase in Complex with 4-Methanesulfonylamino Benzoic Acid

All present enzymatic activity of Ampc Beta-Lactamase in Complex with 4-Methanesulfonylamino Benzoic Acid:
3.5.2.6;

The structure of Ampc Beta-Lactamase in Complex with 4-Methanesulfonylamino Benzoic Acid, PDB code: 2hds was solved by K.Babaoglu, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.16
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.238, 74.764, 98.050, 90.00, 115.98, 90.00
R / Rfree (%)	10.8 / 12.8

The binding sites of Sodium atom in the Ampc Beta-Lactamase in Complex with 4-Methanesulfonylamino Benzoic Acid (pdb code 2hds). 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 Ampc Beta-Lactamase in Complex with 4-Methanesulfonylamino Benzoic Acid, PDB code: 2hds:

Sodium binding site 1 out of 1 in the Ampc Beta-Lactamase in Complex with 4-Methanesulfonylamino Benzoic Acid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Ampc Beta-Lactamase in Complex with 4-Methanesulfonylamino Benzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1501 b:14.7 occ:1.00 O B:HOH1559 2.7 18.5 1.0 OD1 B:ASP217 2.8 11.3 1.0 O B:GLY214 2.9 11.1 1.0 O B:HOH1585 2.9 18.6 1.0 O B:HOH1643 2.9 24.2 1.0 O B:HOH1626 2.9 22.4 1.0 CG B:ASP217 3.6 10.8 1.0 N B:LEU216 3.8 10.5 1.0 C B:GLY214 3.8 10.9 1.0 OD2 B:ASP217 4.0 11.7 1.0 CA B:ALA215 4.0 11.8 1.0 O B:HOH1618 4.1 25.8 1.0 N B:ASP217 4.1 9.3 1.0 C B:ALA215 4.3 10.6 1.0 N B:ALA215 4.4 11.4 1.0 O B:HOH1695 4.5 23.0 1.0 O B:HOH1740 4.6 26.0 1.0 CA B:LEU216 4.6 10.2 1.0 CB B:ASP217 4.7 9.7 1.0 C B:LEU216 4.9 9.4 1.0 N B:GLY214 4.9 11.8 1.0 CA B:ASP217 4.9 9.3 1.0 O B:HOH1642 4.9 24.3 1.0 O B:HOH1930 5.0 35.8 1.0 CA B:GLY214 5.0 11.5 1.0

K.Babaoglu, B.K.Shoichet. Deconstructing Fragment-Based Inhibitor Discovery Nat.Chem.Biol. V. 2 720 2006.
ISSN: ISSN 1552-4450
PubMed: 17072304
DOI: 10.1038/NCHEMBIO831