Chlorine in PDB 3pd9: X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution

The structure of X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution, PDB code: 3pd9 was solved by K.Frydenvang, J.S.Kastrup, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.42 / 2.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.391, 121.251, 47.547, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 23.3

The binding sites of Chlorine atom in the X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution (pdb code 3pd9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution, PDB code: 3pd9:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl266 b:54.0 occ:1.00 NH1 A:ARG160 3.6 59.7 1.0 NH2 A:ARG160 4.3 61.6 1.0 CZ A:ARG160 4.4 61.2 1.0

Chlorine binding site 2 out of 4 in the X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl267 b:64.8 occ:1.00 NE2 A:HIS43 3.6 38.6 0.5 CE1 A:HIS43 3.6 38.6 0.5 NE2 A:GLN241 3.7 28.6 1.0 CD2 A:HIS43 4.3 36.2 0.5 ND1 A:HIS43 4.4 36.2 0.5 NE2 A:HIS43 4.4 35.8 0.5 CE1 A:HIS43 4.5 35.9 0.5 CD A:LYS237 4.6 35.2 1.0 CD A:GLN241 4.7 29.9 1.0 NZ A:LYS237 4.9 52.1 1.0 OE1 A:GLN241 4.9 27.1 1.0

Chlorine binding site 3 out of 4 in the X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl268 b:51.1 occ:1.00 O A:HOH476 3.0 34.0 1.0 O A:ASP136 3.2 34.7 0.5 O A:ASP136 3.2 34.7 0.5 O A:HOH364 3.3 32.4 1.0 NZ A:LYS141 3.5 33.2 1.0 NH2 A:ARG145 3.8 39.0 1.0 CD A:LYS141 3.9 31.5 1.0 CA A:SER137 4.0 28.8 1.0 CE A:LYS141 4.0 34.1 1.0 C A:ASP136 4.2 31.4 0.5 CB A:SER137 4.2 28.3 1.0 C A:ASP136 4.2 31.3 0.5 NH1 A:ARG145 4.3 42.2 1.0 OG A:SER137 4.4 41.5 1.0 CZ A:ARG145 4.6 42.5 1.0 N A:SER137 4.6 28.9 1.0

Chlorine binding site 4 out of 4 in the X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of X-Ray Structure of the Ligand-Binding Core of GLUA2 in Complex with (R)-5-Hpca at 2.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl265 b:55.9 occ:1.00 CE1 B:HIS43 3.2 40.3 0.5 NE2 B:HIS43 3.3 40.4 0.5 NE2 B:GLN241 3.7 36.5 1.0 NZ B:LYS237 3.7 56.8 1.0 CD2 B:HIS43 3.7 40.7 0.5 ND1 B:HIS43 3.8 40.8 0.5 CD B:LYS237 4.0 39.4 1.0 CE B:LYS237 4.3 51.0 1.0 NE2 B:HIS43 4.3 38.5 0.5 CE1 B:HIS43 4.5 38.4 0.5 O B:HOH413 4.5 40.2 1.0 CD B:GLN241 4.8 33.5 1.0

K.Frydenvang, D.S.Pickering, J.R.Greenwood, N.Krogsgaard-Larsen, L.Brehm, B.Nielsen, S.B.Vogensen, H.Hald, J.S.Kastrup, P.Krogsgaard-Larsen, R.P.Clausen. Biostructural and Pharmacological Studies of Bicyclic Analogues of the 3-Isoxazolol Glutamate Receptor Agonist Ibotenic Acid. J. Med. Chem. V. 53 8354 2010.
ISSN: ISSN 1520-4804
PubMed: 21067182
DOI: 10.1021/JM101218A