Zinc in PDB 5tio: Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607

The structure of Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607, PDB code: 5tio was solved by P.L.Shaffer, X.Huang, H.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.25
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	119.120, 119.120, 429.968, 90.00, 90.00, 90.00
R / Rfree (%)	23.3 / 25.4

The binding sites of Zinc atom in the Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607 (pdb code 5tio). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607, PDB code: 5tio:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in the Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn403 b:0.1 occ:0.50 OE2 C:GLU192 2.3 0.6 1.0 NE2 C:HIS215 2.7 0.2 1.0 OD1 C:ASP194 3.0 0.0 1.0 CD2 C:HIS215 3.1 0.5 1.0 OD2 C:ASP194 3.5 0.9 1.0 CD C:GLU192 3.6 0.0 1.0 CE1 C:HIS215 3.6 0.8 1.0 CG C:ASP194 3.7 0.0 1.0 CG C:HIS215 4.2 0.6 1.0 OE1 C:GLU192 4.3 0.8 1.0 ND1 C:HIS215 4.4 0.9 1.0 CG C:GLU192 4.6 0.4 1.0 CB C:GLU192 4.8 0.5 1.0 O C:GLU192 5.0 0.5 1.0

Zinc binding site 2 out of 5 in the Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:0.9 occ:0.50 OD1 A:ASP194 2.6 0.7 1.0 NE2 A:HIS215 2.6 0.7 1.0 OD2 A:ASP194 2.8 0.9 1.0 OE2 A:GLU192 2.8 0.7 1.0 CG A:ASP194 3.1 0.6 1.0 CD2 A:HIS215 3.4 0.5 1.0 CE1 A:HIS215 3.5 0.9 1.0 CD A:GLU192 4.0 0.7 1.0 ND1 A:HIS215 4.5 0.1 1.0 CG A:HIS215 4.5 0.3 1.0 CB A:ASP194 4.6 0.6 1.0 OE1 A:GLU192 4.7 0.6 1.0

Zinc binding site 3 out of 5 in the Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn403 b:0.5 occ:0.50 OE2 B:GLU192 1.9 0.1 1.0 OD1 B:ASP194 2.6 0.7 1.0 NE2 B:HIS215 2.7 0.9 1.0 CD2 B:HIS215 3.1 0.7 1.0 CD B:GLU192 3.1 0.7 1.0 CG B:ASP194 3.4 0.7 1.0 OD2 B:ASP194 3.4 0.2 1.0 CE1 B:HIS215 3.8 0.4 1.0 OE1 B:GLU192 3.9 0.5 1.0 CG B:GLU192 4.1 0.2 1.0 CG B:HIS215 4.3 0.6 1.0 CB B:GLU192 4.3 0.4 1.0 O B:GLU192 4.5 0.6 1.0 ND1 B:HIS215 4.6 0.2 1.0 CB B:ASP194 4.8 0.5 1.0 N B:ASP194 4.9 0.6 1.0 C B:GLU192 4.9 0.7 1.0

Zinc binding site 4 out of 5 in the Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn403 b:0.9 occ:0.50 OE2 D:GLU192 2.0 0.8 1.0 NE2 D:HIS215 2.7 0.7 1.0 OD1 D:ASP194 2.8 0.2 1.0 CD2 D:HIS215 3.0 0.0 1.0 CD D:GLU192 3.2 0.6 1.0 OD2 D:ASP194 3.5 0.8 1.0 CG D:ASP194 3.5 0.5 1.0 CE1 D:HIS215 3.8 0.2 1.0 OE1 D:GLU192 4.0 0.8 1.0 CG D:HIS215 4.2 0.0 1.0 CG D:GLU192 4.2 0.5 1.0 CB D:GLU192 4.4 0.4 1.0 ND1 D:HIS215 4.5 0.1 1.0 O D:GLU192 4.6 0.7 1.0 CB D:ASP194 5.0 1.0 1.0

Zinc binding site 5 out of 5 in the Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Human Glycine Receptor Alpha-3 Bound to Am-3607 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn403 b:0.2 occ:0.50 OE2 E:GLU192 2.4 0.6 1.0 OD1 E:ASP194 2.6 0.6 1.0 NE2 E:HIS215 2.9 0.2 1.0 OD2 E:ASP194 3.1 0.8 1.0 CG E:ASP194 3.2 0.7 1.0 CD2 E:HIS215 3.5 0.5 1.0 CD E:GLU192 3.7 0.7 1.0 CE1 E:HIS215 3.8 0.5 1.0 OE1 E:GLU192 4.3 1.0 1.0 CG E:HIS215 4.6 0.9 1.0 CB E:ASP194 4.7 0.9 1.0 ND1 E:HIS215 4.7 0.5 1.0 CG E:GLU192 4.7 0.9 1.0

X.Huang, P.L.Shaffer, S.Ayube, H.Bregman, H.Chen, S.G.Lehto, J.A.Luther, D.J.Matson, S.I.Mcdonough, K.Michelsen, M.M.Plant, S.Schneider, J.R.Simard, Y.Teffera, S.Yi, M.Zhang, E.F.Dimauro, J.Gingras. Crystal Structures of Human GLYRA3 Bound to A Novel Class of Potentiators with Efficacy in A Mouse Model of Neuropathic Pain To Be Published.