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

Enzymatic activity of 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;

Protein crystallography data

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 / R_free (%)*	19.8 / 26.3

Other elements in 1nva:

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

Zinc

(Zn)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Adp, PDB code: 1nva:

Chlorine binding site 1 out of 1 in 1nva

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Chlorine Binding Sites List in 1nva

Chlorine binding site 1 out of 1 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 Chlorine with other atoms in the Cl 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:Cl602 b:63.1 occ:1.00	NZ	A:LYS89	3.2	28.3	1.0
	CZ	A:PHE123	3.6	42.9	1.0
	NZ	B:LYS89	3.7	23.0	1.0
	CE	A:LYS89	3.7	25.8	1.0
	CE2	A:PHE123	3.9	25.4	1.0
	CZ	B:PHE123	3.9	24.8	1.0
	O	A:HOH1455	4.0	41.6	1.0
	CD	A:LYS89	4.2	17.7	1.0
	CE	B:LYS89	4.2	22.0	1.0
	CE2	B:PHE123	4.3	37.4	1.0
	CE1	A:PHE123	4.6	28.1	1.0
	CD	B:LYS89	4.7	19.8	1.0
	OG1	A:THR127	4.7	52.1	1.0
	OG1	B:THR127	4.8	37.7	1.0
	CE1	B:PHE123	4.9	33.0	1.0
	CG2	A:ILE164	4.9	56.8	1.0
	CG2	B:THR127	4.9	17.7	1.0
	CG2	A:THR127	4.9	36.0	1.0

Reference:

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

Page generated: Thu Jul 10 18:33:12 2025

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