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Chlorine in PDB 1lik: Structure of T. Gondii Adenosine Kinase Bound to Adenosine

Enzymatic activity of Structure of T. Gondii Adenosine Kinase Bound to Adenosine

All present enzymatic activity of Structure of T. Gondii Adenosine Kinase Bound to Adenosine:
2.7.1.20;

Protein crystallography data

The structure of Structure of T. Gondii Adenosine Kinase Bound to Adenosine, PDB code: 1lik was solved by M.A.Schumacher, D.M.Scott, I.I.Mathews, S.E.Ealick, D.S.Roos, B.Ullman, R.G.Brennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.55
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 168.200, 47.010, 44.430, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of T. Gondii Adenosine Kinase Bound to Adenosine (pdb code 1lik). 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 Structure of T. Gondii Adenosine Kinase Bound to Adenosine, PDB code: 1lik:

Chlorine binding site 1 out of 1 in 1lik

Go back to Chlorine Binding Sites List in 1lik
Chlorine binding site 1 out of 1 in the Structure of T. Gondii Adenosine Kinase Bound to Adenosine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of T. Gondii Adenosine Kinase Bound to Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl899

b:84.2
occ:1.00
CE A:LYS80 3.3 0.0 1.0
NH2 A:ARG83 4.1 0.0 1.0
NZ A:LYS80 4.1 0.0 1.0
O A:HOH1005 4.2 43.8 1.0
CZ A:ARG83 4.3 60.8 1.0
O A:LYS80 4.5 26.9 1.0
CD A:LYS80 4.6 76.1 1.0
NE A:ARG83 4.6 41.1 1.0
CG A:LYS80 4.6 51.8 1.0
NH1 A:ARG83 4.9 45.7 1.0

Reference:

M.A.Schumacher, D.M.Scott, I.I.Mathews, S.E.Ealick, D.S.Roos, B.Ullman, R.G.Brennan. Crystal Structures of Toxoplasma Gondii Adenosine Kinase Reveal A Novel Catalytic Mechanism and Prodrug Binding. J.Mol.Biol. V. 298 875 2000.
ISSN: ISSN 0022-2836
PubMed: 10801355
DOI: 10.1006/JMBI.2000.3753
Page generated: Fri Jul 19 23:50:52 2024

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