Zinc in PDB 1nr5: Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate

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

The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate, PDB code: 1nr5 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)	27.22 / 2.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	133.990, 86.560, 74.820, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 23.2

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

Cobalt	(Co)	1 atom
Chlorine	(Cl)	2 atoms

The binding sites of Zinc atom in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate (pdb code 1nr5). 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+, Nad and Carbaphosphonate, PDB code: 1nr5:
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+, Nad and Carbaphosphonate


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+, Nad and Carbaphosphonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn600 b:27.8 occ:1.00 OE2 A:GLU194 2.0 13.7 1.0 O4 A:CRB1500 2.1 21.7 1.0 NE2 A:HIS271 2.2 19.3 1.0 NE2 A:HIS287 2.2 18.8 1.0 O5 A:CRB1500 2.3 20.0 1.0 C4 A:CRB1500 2.9 19.6 1.0 C5 A:CRB1500 3.0 16.8 1.0 CD A:GLU194 3.1 25.5 1.0 CE1 A:HIS271 3.1 19.6 1.0 CD2 A:HIS287 3.1 17.2 1.0 CD2 A:HIS271 3.2 23.3 1.0 CE1 A:HIS287 3.3 17.4 1.0 C5N A:NAD400 3.4 21.6 1.0 OE1 A:GLU194 3.4 23.2 1.0 C6N A:NAD400 3.8 24.0 1.0 OD2 A:ASP146 3.8 28.2 1.0 CG2 A:VAL291 4.1 24.7 1.0 ND1 A:HIS271 4.3 23.7 1.0 O A:HOH1532 4.3 28.4 1.0 C4N A:NAD400 4.3 27.5 1.0 CG A:HIS271 4.3 22.5 1.0 CG A:HIS287 4.3 19.6 1.0 C3 A:CRB1500 4.3 20.1 1.0 CG A:GLU194 4.4 13.3 1.0 ND1 A:HIS287 4.4 15.6 1.0 C6 A:CRB1500 4.4 14.1 1.0 NZ A:LYS197 4.7 22.5 1.0 N1N A:NAD400 5.0 22.3 1.0 CG A:ASP146 5.0 16.4 1.0

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


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+, Nad and Carbaphosphonate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:34.8 occ:1.00 OE2 B:GLU194 2.0 26.3 1.0 NE2 B:HIS271 2.1 16.7 1.0 NE2 B:HIS287 2.3 20.4 1.0 O5 B:CRB1501 2.3 32.1 1.0 O4 B:CRB1501 2.4 25.2 1.0 CE1 B:HIS271 3.0 25.9 1.0 CD B:GLU194 3.0 31.8 1.0 C4 B:CRB1501 3.0 20.6 1.0 C5 B:CRB1501 3.1 31.3 1.0 CD2 B:HIS271 3.1 19.6 1.0 CD2 B:HIS287 3.2 25.9 1.0 CE1 B:HIS287 3.4 19.4 1.0 OE1 B:GLU194 3.4 25.2 1.0 C5N B:NAD401 3.5 36.3 1.0 OD2 B:ASP146 3.8 25.2 1.0 C6N B:NAD401 3.9 32.8 1.0 CG2 B:VAL291 4.0 22.8 1.0 ND1 B:HIS271 4.1 23.1 1.0 CG B:HIS271 4.2 26.4 1.0 CG B:GLU194 4.3 25.9 1.0 CG B:HIS287 4.4 24.2 1.0 O B:HOH1503 4.4 22.9 1.0 C4N B:NAD401 4.4 42.1 1.0 ND1 B:HIS287 4.4 24.1 1.0 C6 B:CRB1501 4.5 33.1 1.0 C3 B:CRB1501 4.5 20.5 1.0 NZ B:LYS197 4.7 22.4 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