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Atomistry » Zinc » PDB 4zw3-5a22 » 4zya | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4zw3-5a22 » 4zya » |
Zinc in PDB 4zya: The N-Terminal Extension Domain of Human Asparaginyl-Trna SynthetaseEnzymatic activity of The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase
All present enzymatic activity of The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase:
6.1.1.22; Protein crystallography data
The structure of The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase, PDB code: 4zya
was solved by
J.S.Park,
M.C.Park,
P.Goughnour,
H.S.Kim,
S.J.Kim,
H.J.Kim,
S.H.Kim,
B.W.Han,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4zya:
The structure of The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase
(pdb code 4zya). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase, PDB code: 4zya: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 4zyaGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 4zyaGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the The N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase
![]() Mono view ![]() Stereo pair view
Reference:
J.S.Park,
M.C.Park,
K.Y.Lee,
P.C.Goughnour,
S.J.Jeong,
H.S.Kim,
H.J.Kim,
B.J.Lee,
S.Kim,
B.W.Han.
Unique N-Terminal Extension Domain of Human Asparaginyl-Trna Synthetase Elicits CCR3-Mediated Chemokine Activity. Int. J. Biol. Macromol. V. 120 835 2018.
Page generated: Sun Oct 27 12:09:26 2024
ISSN: ISSN 1879-0003 PubMed: 30171954 DOI: 10.1016/J.IJBIOMAC.2018.08.171 |
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