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Chlorine in PDB 1dqs: Crystal Structure of Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+

Enzymatic activity of Crystal Structure of Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+

All present enzymatic activity of Crystal Structure of Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+:
4.6.1.3;

Protein crystallography data

The structure of Crystal Structure of Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+, PDB code: 1dqs was solved by E.P.Carpenter, A.R.Hawkins, J.W.Frost, K.A.Brown, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.677, 80.810, 143.513, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 22.4

Other elements in 1dqs:

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

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+ (pdb code 1dqs). 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 Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+, PDB code: 1dqs:

Chlorine binding site 1 out of 1 in 1dqs

Go back to Chlorine Binding Sites List in 1dqs
Chlorine binding site 1 out of 1 in the Crystal Structure of Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+


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 Dehydroquinate Synthase (Dhqs) Complexed with Carbaphosphonate, Nad+ and ZN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:19.2
occ:1.00
 O A:HOH558 3.0 17.7 1.0
NZ A:LYS89 3.0 14.6 1.0
O A:HOH1058 3.1 15.7 1.0
NZ B:LYS89 3.2 11.9 1.0
CZ B:PHE123 3.8 11.9 1.0
CZ A:PHE123 3.9 13.3 1.0
CE A:LYS89 3.9 15.4 1.0
CE B:LYS89 3.9 13.2 1.0
CD A:LYS89 4.2 14.6 1.0
CE2 B:PHE123 4.3 12.4 1.0
CE2 A:PHE123 4.3 12.3 1.0
CD B:LYS89 4.4 13.1 1.0
O A:HOH514 4.4 15.8 1.0
O B:HOH1014 4.5 17.6 1.0
CE1 B:PHE123 4.6 12.4 1.0
CE1 A:PHE123 4.6 10.7 1.0
OG1 A:THR127 4.7 12.4 1.0
O A:HOH524 4.7 14.2 1.0
O B:HOH1024 4.8 17.2 1.0
CG2 A:THR127 4.8 9.1 1.0
OG1 B:THR127 4.9 12.1 1.0
CG2 B:THR127 4.9 10.3 1.0

Reference:

E.P.Carpenter, A.R.Hawkins, J.W.Frost, K.A.Brown. Structure of Dehydroquinate Synthase Reveals An Active Site Capable of Multistep Catalysis. Nature V. 394 299 1998.
ISSN: ISSN 0028-0836
PubMed: 9685163
DOI: 10.1038/28431
Page generated: Fri Jul 19 21:37:42 2024

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