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Atomistry » Nickel » PDB 3qsi-3tsn » 3str | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Nickel » PDB 3qsi-3tsn » 3str » |
Nickel in PDB 3str: Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic AcidEnzymatic activity of Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic Acid
All present enzymatic activity of Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic Acid:
3.5.1.88; Protein crystallography data
The structure of Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic Acid, PDB code: 3str
was solved by
N.Campobasso,
P.Ward,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3str:
The structure of Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic Acid also contains other interesting chemical elements:
Nickel Binding Sites:
The binding sites of Nickel atom in the Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic Acid
(pdb code 3str). This binding sites where shown within
5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic Acid, PDB code: 3str: Nickel binding site 1 out of 1 in 3strGo back to Nickel Binding Sites List in 3str
Nickel binding site 1 out
of 1 in the Strep Peptide Deformylase with A Time Dependent Thiazolidine Hydroxamic Acid
Mono view Stereo pair view
Reference:
R.Totoritis,
C.Duraiswami,
A.N.Taylor,
J.J.Kerrigan,
N.Campobasso,
K.J.Smith,
P.Ward,
B.W.King,
M.Murrayz-Thompson,
A.D.Jones,
G.S.Van Aller,
K.M.Aubart,
M.Zalacain,
S.H.Thrall,
T.D.Meek,
B.Schwartz.
Understanding the Origins of Time-Dependent Inhibition By Polypeptide Deformylase Inhibitors. Biochemistry V. 50 6642 2011.
Page generated: Wed Dec 16 01:27:41 2020
ISSN: ISSN 0006-2960 PubMed: 21711014 DOI: 10.1021/BI200655G |
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