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

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

The structure of Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad+ and Carbaphosphonate, PDB code: 1xai was solved by C.E.Nichols, J.Ren, K.Leslie, B.Dhaliwal, M.Lockyer, I.Charles, 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)	24.01 / 2.30
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	54.898, 54.898, 229.111, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 31.2

The binding sites of Zinc atom in the Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad+ and Carbaphosphonate (pdb code 1xai). 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 Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad+ and Carbaphosphonate, PDB code: 1xai:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Staphlyococcus Aureus 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 Staphlyococcus Aureus 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:37.7 occ:1.00 OE1 A:GLU178 2.2 25.4 1.0 NE2 A:HIS256 2.2 23.1 1.0 NE2 A:HIS242 2.2 25.8 1.0 O4 A:CRB500 2.3 48.5 1.0 O5 A:CRB500 2.4 28.9 1.0 CD2 A:HIS242 3.0 37.0 1.0 C4 A:CRB500 3.0 37.8 1.0 CD2 A:HIS256 3.1 25.5 1.0 C5 A:CRB500 3.2 39.5 1.0 CD A:GLU178 3.2 25.7 1.0 CE1 A:HIS256 3.3 22.9 1.0 CE1 A:HIS242 3.4 16.9 1.0 O A:HOH631 3.4 44.1 1.0 OE2 A:GLU178 3.6 36.0 1.0 OD2 A:ASP130 3.8 52.2 1.0 CG2 A:VAL260 4.1 8.9 1.0 CG A:HIS242 4.2 39.3 1.0 CG A:HIS256 4.3 29.2 1.0 ND1 A:HIS256 4.3 33.6 1.0 ND1 A:HIS242 4.3 29.9 1.0 CG A:GLU178 4.5 10.8 1.0 C3 A:CRB500 4.5 35.3 1.0 C6 A:CRB500 4.6 49.3 1.0 NZ A:LYS181 4.7 16.0 1.0 O A:HOH630 4.7 36.3 1.0 CG A:ASP130 4.9 37.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Staphlyococcus Aureus 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 Staphlyococcus Aureus 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:34.5 occ:1.00 NE2 B:HIS242 2.1 29.3 1.0 O4 B:CRB501 2.2 43.1 1.0 NE2 B:HIS256 2.3 29.9 1.0 OE1 B:GLU178 2.3 31.5 1.0 O5 B:CRB501 2.5 31.9 1.0 CD2 B:HIS242 3.0 34.2 1.0 C4 B:CRB501 3.0 41.9 1.0 CD2 B:HIS256 3.1 34.1 1.0 CD B:GLU178 3.2 33.6 1.0 CE1 B:HIS242 3.2 30.0 1.0 C5 B:CRB501 3.2 40.0 1.0 CE1 B:HIS256 3.3 34.5 1.0 OE2 B:GLU178 3.4 31.5 1.0 O B:HOH714 3.6 72.8 1.0 OD2 B:ASP130 3.7 48.4 1.0 CG B:HIS242 4.2 35.3 1.0 CG2 B:VAL260 4.2 12.3 1.0 ND1 B:HIS242 4.3 29.1 1.0 CG B:HIS256 4.3 36.4 1.0 ND1 B:HIS256 4.4 45.1 1.0 C3 B:CRB501 4.4 27.7 1.0 CG B:GLU178 4.5 17.3 1.0 C6 B:CRB501 4.6 42.2 1.0 NZ B:LYS181 4.8 24.4 1.0 CG B:ASP130 4.8 37.1 1.0

C.E.Nichols, J.Ren, K.Leslie, B.Dhaliwal, M.Lockyer, I.Charles, A.R.Hawkins, D.K.Stammers. Comparison of Ligand Induced Conformational Changes and Domain Closure Mechanisms, Between Prokaryotic and Eukaryotic Dehydroquinate Synthases. J.Mol.Biol. V. 343 533 2004.
ISSN: ISSN 0022-2836
PubMed: 15465043
DOI: 10.1016/J.JMB.2004.08.039