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Atomistry » Zinc » PDB 3lju-3lt9 » 3lkm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3lju-3lt9 » 3lkm » |
Zinc in PDB 3lkm: 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with AmpEnzymatic activity of 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with Amp
All present enzymatic activity of 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with Amp:
2.7.11.7; Protein crystallography data
The structure of 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with Amp, PDB code: 3lkm
was solved by
Q.Ye,
Z.Jia,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3lkm:
The structure of 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with Amp also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with Amp
(pdb code 3lkm). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with Amp, PDB code: 3lkm: Zinc binding site 1 out of 1 in 3lkmGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the 1.6 Angstrom Crystal Structure of the Alpha-Kinase Domain of Myosin Heavy Chain Kinase A Complex with Amp
![]() Mono view ![]() Stereo pair view
Reference:
Q.Ye,
S.W.Crawley,
Y.Yang,
G.P.Cote,
Z.Jia.
Crystal Structure of the {Alpha}-Kinase Domain of Dictyostelium Myosin Heavy Chain Kinase A. Sci.Signal. V. 3 RA17 2010.
Page generated: Sat Oct 26 08:41:04 2024
ISSN: ESSN 1937-9145 PubMed: 20197546 DOI: 10.1126/SCISIGNAL.2000525 |
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