Chlorine in PDB 2ze5: Crystal Structure of Adenosine Phosphate-Isopentenyltransferase

All present enzymatic activity of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase:
2.5.1.27;

The structure of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase, PDB code: 2ze5 was solved by H.Sakakibara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.20 / 2.31
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.392, 96.392, 65.197, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 25.4

The binding sites of Chlorine atom in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase (pdb code 2ze5). 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 Adenosine Phosphate-Isopentenyltransferase, PDB code: 2ze5:

Chlorine binding site 1 out of 1 in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase


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 Adenosine Phosphate-Isopentenyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:61.6 occ:1.00 CG A:LYS14 3.3 49.6 1.0 N A:LYS14 3.4 47.6 1.0 CE A:LYS14 3.5 46.8 1.0 N A:GLY13 3.6 50.3 1.0 N A:SER12 3.7 50.3 1.0 N A:THR15 3.7 48.1 1.0 CD A:LYS14 3.7 48.6 1.0 N A:CYS11 4.0 48.0 1.0 CB A:LYS14 4.0 46.8 1.0 C A:GLY13 4.0 49.8 1.0 CA A:GLY13 4.1 49.9 1.0 CA A:LYS14 4.1 48.2 1.0 NZ A:LYS14 4.3 43.5 1.0 OG1 A:THR15 4.3 47.4 1.0 CA A:CYS11 4.3 48.6 1.0 C A:SER12 4.3 50.9 1.0 C A:CYS11 4.4 48.5 1.0 C A:LYS14 4.5 47.4 1.0 CA A:SER12 4.5 51.0 1.0 CB A:THR15 4.5 46.8 1.0 CA A:THR15 4.7 47.7 1.0 O A:PRO9 4.7 42.9 1.0 C A:THR10 4.9 47.8 1.0 CB A:SER12 4.9 52.4 1.0

H.Sugawara, N.Ueda, M.Kojima, N.Makita, T.Yamaya, H.Sakakibara. Structural Insight Into the Reaction Mechanism and Evolution of Cytokinin Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 105 2734 2008.
ISSN: ISSN 0027-8424
PubMed: 18258747
DOI: 10.1073/PNAS.0707374105