Zinc in PDB 3t9v: Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2

The structure of Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9v was solved by A.H.Ahmed, R.E.Oswald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.60 / 1.98
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.162, 58.704, 96.072, 90.00, 93.41, 90.00
R / Rfree (%)	17.8 / 23.8

The binding sites of Zinc atom in the Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 (pdb code 3t9v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9v:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:50.7 occ:1.00 NE2 A:HIS23 2.2 36.9 1.0 O A:HOH421 2.6 42.0 1.0 CD2 A:HIS23 3.2 30.2 1.0 CE1 A:HIS23 3.3 36.5 1.0 CG A:HIS23 4.3 31.0 1.0 ND1 A:HIS23 4.4 33.7 1.0 O A:HOH310 4.7 34.8 1.0

Zinc binding site 2 out of 4 in the Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:32.1 occ:1.00 OE1 A:GLU42 2.2 31.4 1.0 NE2 A:HIS46 2.7 31.9 1.0 OE2 A:GLU42 2.8 29.4 1.0 CD A:GLU42 2.9 27.5 1.0 CE1 A:HIS46 3.6 36.5 1.0 CD2 A:HIS46 3.7 30.0 1.0 OE1 A:GLN244 4.2 32.6 1.0 CD1 A:LEU246 4.3 33.5 1.0 CD2 A:LEU241 4.3 24.8 1.0 CG A:GLU42 4.3 26.3 1.0 CD A:LYS45 4.7 38.9 1.0 ND1 A:HIS46 4.8 34.7 1.0 CG A:HIS46 4.8 32.9 1.0 CB A:GLU42 4.9 25.6 1.0

Zinc binding site 3 out of 4 in the Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn3 b:52.9 occ:1.00 OE2 B:GLU24 2.2 49.8 1.0 NE2 B:HIS23 2.4 40.1 1.0 O B:HOH360 2.5 40.3 1.0 O B:HOH461 2.8 22.8 1.0 CD B:GLU24 3.1 46.4 1.0 CD2 B:HIS23 3.2 36.0 1.0 CG B:GLU24 3.3 41.5 1.0 CE1 B:HIS23 3.4 39.3 1.0 O B:HOH361 3.5 41.4 1.0 OE1 B:GLU24 4.3 49.9 1.0 CG B:HIS23 4.4 34.0 1.0 ND1 B:HIS23 4.5 34.5 1.0 O B:HOH498 4.6 43.3 1.0 CB B:GLU24 4.8 43.9 1.0

Zinc binding site 4 out of 4 in the Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cnqx Bound to A Reduced Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn262 b:29.0 occ:1.00 NE2 B:HIS46 2.4 27.2 1.0 OE2 B:GLU42 2.5 27.5 1.0 CE1 B:HIS46 3.3 31.6 1.0 CD B:GLU42 3.3 27.2 1.0 OE1 B:GLU42 3.4 33.1 1.0 CD2 B:HIS46 3.5 25.4 1.0 OE1 B:GLN244 3.5 33.2 1.0 CD2 B:LEU241 4.0 20.2 1.0 O B:HOH410 4.4 39.5 1.0 ND1 B:HIS46 4.4 29.3 1.0 CD B:GLN244 4.5 36.6 1.0 CG B:HIS46 4.6 29.1 1.0 NE2 B:GLN244 4.6 43.1 1.0 CG B:GLU42 4.7 23.4 1.0 CD B:LYS45 4.9 32.6 1.0

A.H.Ahmed, S.Wang, H.H.Chuang, R.E.Oswald. Mechanism of Ampa Receptor Activation By Partial Agonists: Disulfide Trapping of Closed Lobe Conformations. J.Biol.Chem. V. 286 35257 2011.
ISSN: ISSN 0021-9258
PubMed: 21846932
DOI: 10.1074/JBC.M111.269001