Zinc in PDB 1nua: Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+

All present enzymatic activity of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+:
4.2.3.4;

The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, PDB code: 1nua was solved by C.E.Nichols, J.Ren, H.K.Lamb, A.R.Hawkins, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.72 / 2.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	40.590, 68.320, 135.030, 90.00, 84.69, 90.00
R / Rfree (%)	18.2 / 26.9

The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ (pdb code 1nua). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, PDB code: 1nua:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+


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 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn600 b:50.7 occ:1.00 OE2 A:GLU194 2.1 31.9 1.0 NE2 A:HIS271 2.3 23.6 1.0 NE2 A:HIS287 2.3 31.4 1.0 CD A:GLU194 3.1 29.9 1.0 CE1 A:HIS287 3.2 30.8 1.0 CD2 A:HIS271 3.2 30.1 1.0 CE1 A:HIS271 3.3 30.7 1.0 CD2 A:HIS287 3.3 31.6 1.0 O A:HOH602 3.5 13.3 1.0 OE1 A:GLU194 3.5 25.3 1.0 OD2 A:ASP146 3.5 45.8 1.0 ND1 A:HIS287 4.3 10.4 1.0 CG A:HIS271 4.4 20.8 1.0 CG A:GLU194 4.4 26.4 1.0 ND1 A:HIS271 4.4 16.6 1.0 CG A:HIS287 4.4 14.1 1.0 CG A:ASP146 4.5 42.8 1.0 O A:HOH787 4.6 13.6 1.0 NZ A:LYS197 4.8 23.5 1.0 O A:HOH768 4.8 43.7 1.0 CG2 A:VAL291 4.8 17.5 1.0 OD1 A:ASP146 5.0 50.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+


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 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:45.5 occ:1.00 NE2 B:HIS287 2.1 26.1 1.0 OE2 B:GLU194 2.2 33.4 1.0 NE2 B:HIS271 2.3 24.1 1.0 O B:HOH647 2.7 25.6 1.0 CE1 B:HIS287 3.0 21.6 1.0 CD2 B:HIS271 3.2 25.7 1.0 CD2 B:HIS287 3.2 25.7 1.0 CD B:GLU194 3.2 34.6 1.0 CE1 B:HIS271 3.3 27.1 1.0 O B:HOH691 3.6 42.2 1.0 O B:HOH628 3.6 52.9 1.0 OE1 B:GLU194 3.7 37.0 1.0 OD2 B:ASP146 3.8 43.5 1.0 ND1 B:HIS287 4.1 10.0 1.0 CG B:HIS287 4.2 19.3 1.0 CG B:HIS271 4.4 33.0 1.0 ND1 B:HIS271 4.4 36.0 1.0 CG B:GLU194 4.5 29.1 1.0 O B:HOH692 4.5 35.1 1.0 CG2 B:VAL291 4.7 34.0 1.0 CG B:ASP146 4.8 46.6 1.0

C.E.Nichols, J.Ren, H.K.Lamb, A.R.Hawkins, D.K.Stammers. Ligand-Induced Conformational Changes and A Mechanism For Domain Closure in Aspergillus Nidulans Dehydroquinate Synthase J.Mol.Biol. V. 327 129 2003.
ISSN: ISSN 0022-2836
PubMed: 12614613
DOI: 10.1016/S0022-2836(03)00086-X