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Atomistry » Zinc » PDB 3ciz-3cyu » 3cpm » |
Zinc in PDB 3cpm: Plant Peptide Deformylase PDF1B Crystal StructureEnzymatic activity of Plant Peptide Deformylase PDF1B Crystal Structure
All present enzymatic activity of Plant Peptide Deformylase PDF1B Crystal Structure:
3.5.1.88; Protein crystallography data
The structure of Plant Peptide Deformylase PDF1B Crystal Structure, PDB code: 3cpm
was solved by
D.W.Rodgers,
R.L.Houtz,
L.M.A.Dirk,
J.J.Schmidt,
Y.Cai,
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 Plant Peptide Deformylase PDF1B Crystal Structure
(pdb code 3cpm). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Plant Peptide Deformylase PDF1B Crystal Structure, PDB code: 3cpm: Jump to Zinc binding site number: 1; 2; 3; 4; Zinc binding site 1 out of 4 in 3cpmGo back to Zinc Binding Sites List in 3cpm
Zinc binding site 1 out
of 4 in the Plant Peptide Deformylase PDF1B Crystal Structure
Mono view Stereo pair view
Zinc binding site 2 out of 4 in 3cpmGo back to Zinc Binding Sites List in 3cpm
Zinc binding site 2 out
of 4 in the Plant Peptide Deformylase PDF1B Crystal Structure
Mono view Stereo pair view
Zinc binding site 3 out of 4 in 3cpmGo back to Zinc Binding Sites List in 3cpm
Zinc binding site 3 out
of 4 in the Plant Peptide Deformylase PDF1B Crystal Structure
Mono view Stereo pair view
Zinc binding site 4 out of 4 in 3cpmGo back to Zinc Binding Sites List in 3cpm
Zinc binding site 4 out
of 4 in the Plant Peptide Deformylase PDF1B Crystal Structure
Mono view Stereo pair view
Reference:
L.M.Dirk,
J.J.Schmidt,
Y.Cai,
J.C.Barnes,
K.M.Hanger,
N.R.Nayak,
M.A.Williams,
R.B.Grossman,
R.L.Houtz,
D.W.Rodgers.
Insights Into the Substrate Specificity of Plant Peptide Deformylase, An Essential Enzyme with Potential For the Development of Novel Biotechnology Applications in Agriculture Biochem.J. V. 413 417 2008.
Page generated: Wed Dec 16 04:11:11 2020
ISSN: ISSN 0264-6021 PubMed: 18412546 DOI: 10.1042/BJ20071641 |
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