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Atomistry » Zinc » PDB 2z45-2zem » 2ze7 » |
Zinc in PDB 2ze7: Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, DmasppEnzymatic activity of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp
All present enzymatic activity of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp:
2.5.1.27; Protein crystallography data
The structure of Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp, PDB code: 2ze7
was solved by
H.Sakakibara,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp
(pdb code 2ze7). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp, PDB code: 2ze7: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2ze7Go back to Zinc Binding Sites List in 2ze7
Zinc binding site 1 out
of 2 in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2ze7Go back to Zinc Binding Sites List in 2ze7
Zinc binding site 2 out
of 2 in the Crystal Structure of Adenosine Phosphate-Isopentenyltransferase Complexed with Zinc Ion and Substrate Analog, Dmaspp
Mono view Stereo pair view
Reference:
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.
Page generated: Thu Oct 24 10:45:06 2024
ISSN: ISSN 0027-8424 PubMed: 18258747 DOI: 10.1073/PNAS.0707374105 |
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