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

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

The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Adp, PDB code: 1nva 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)	30.00 / 2.62
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.010, 68.910, 137.710, 90.00, 94.71, 90.00
R / Rfree (%)	19.8 / 26.3

The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Adp 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+ and Adp (pdb code 1nva). 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+ and Adp, PDB code: 1nva:
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+ and Adp


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+ and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn600 b:56.2 occ:1.00 OE1 A:GLU194 2.0 44.7 1.0 NE2 A:HIS271 2.2 39.2 1.0 NE2 A:HIS287 2.3 40.7 1.0 CD A:GLU194 3.0 44.2 1.0 CE1 A:HIS271 3.0 46.6 1.0 CD2 A:HIS287 3.2 31.7 1.0 CD2 A:HIS271 3.3 42.5 1.0 OE2 A:GLU194 3.3 38.5 1.0 CE1 A:HIS287 3.4 30.9 1.0 OD2 A:ASP146 3.7 41.1 1.0 ND1 A:HIS271 4.2 49.7 1.0 CG A:GLU194 4.2 41.7 1.0 CG A:HIS271 4.4 41.0 1.0 CG A:HIS287 4.4 30.9 1.0 ND1 A:HIS287 4.4 26.3 1.0 CG2 A:VAL291 4.5 19.6 1.0 NZ A:LYS197 4.8 39.1 1.0 CG A:ASP146 4.9 46.1 1.0

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


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+ and Adp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:47.3 occ:1.00 NE2 B:HIS271 2.0 22.5 1.0 OE1 B:GLU194 2.1 42.6 1.0 NE2 B:HIS287 2.3 49.5 1.0 CE1 B:HIS271 2.9 21.4 1.0 CD B:GLU194 3.1 39.6 1.0 CD2 B:HIS271 3.1 16.2 1.0 CD2 B:HIS287 3.2 45.1 1.0 CE1 B:HIS287 3.3 28.4 1.0 OE2 B:GLU194 3.4 40.1 1.0 OD2 B:ASP146 3.8 42.9 1.0 ND1 B:HIS271 4.1 19.6 1.0 CG B:HIS271 4.2 30.9 1.0 CG B:GLU194 4.3 34.0 1.0 CG B:HIS287 4.4 38.2 1.0 ND1 B:HIS287 4.4 35.9 1.0 CG2 B:VAL291 4.4 34.3 1.0 O B:HOH1448 4.7 52.1 1.0 NZ B:LYS197 4.8 38.9 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