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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1nr5:

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

Chlorine (Cl) 2 atoms
Zinc (Zn) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt 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 Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate, PDB code: 1nr5:

Cobalt binding site 1 out of 1 in 1nr5

Go back to Cobalt Binding Sites List in 1nr5
Cobalt binding site 1 out of 1 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 Cobalt with other atoms in the Co 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
B:Co602

b:78.0
occ:1.00
 NH2 B:ARG303 3.7 50.0 1.0
NE B:ARG303 3.8 44.2 1.0
N B:GLY310 3.9 42.5 1.0
CZ B:ARG303 4.2 47.5 1.0
CA B:GLY310 4.6 35.6 1.0
CA B:LYS309 4.8 43.3 1.0
C B:LYS309 4.9 43.8 1.0
CG B:LYS309 4.9 66.5 1.0
CG B:ARG303 4.9 39.0 1.0
CD B:ARG303 4.9 45.0 1.0
CE A:LYS309 4.9 62.2 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: Tue Jul 30 14:27:15 2024

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