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

Enzymatic activity of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Carbaphosphonate

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

Protein crystallography data

The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Carbaphosphonate, PDB code: 1nvd 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 / 2.51
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	64.030, 70.030, 197.630, 90.00, 90.00, 90.00
*R / R_free (%)*	19.6 / 26.7

Other elements in 1nvd:

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

Chlorine binding site 1 out of 1 in 1nvd

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Chlorine Binding Sites List in 1nvd

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

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 Carbaphosphonate within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl602 b:32.0 occ:1.00	O	A:HOH616	2.8	10.6	1.0
	NZ	B:LYS89	3.2	20.7	1.0
	NZ	A:LYS89	3.2	15.8	1.0
	O	B:HOH602	3.3	13.6	1.0
	CE	A:LYS89	3.6	17.3	1.0
	CZ	A:PHE123	3.8	16.0	1.0
	CE	B:LYS89	3.9	21.4	1.0
	CD	A:LYS89	4.0	22.9	1.0
	CZ	B:PHE123	4.1	15.7	1.0
	CE2	A:PHE123	4.2	24.4	1.0
	O	A:HOH629	4.2	34.2	1.0
	CD	B:LYS89	4.3	17.3	1.0
	CE2	B:PHE123	4.5	23.3	1.0
	O	A:HOH669	4.6	27.9	1.0
	CE1	A:PHE123	4.7	17.8	1.0
	O	B:HOH663	4.7	25.2	1.0
	OG1	A:THR127	4.8	15.9	1.0
	CE1	B:PHE123	4.9	20.2	1.0
	OG1	B:THR127	4.9	10.8	1.0
	CG2	A:THR127	4.9	8.6	1.0
	CG2	A:ILE164	4.9	22.1	1.0
	CG2	B:THR127	5.0	13.1	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 18:33:26 2025

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