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Atomistry » Zinc » PDB 6a57-6agg » 6a8z | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 6a57-6agg » 6a8z » |
Zinc in PDB 6a8z: Crystal Structure of M1 Zinc Metallopeptidase From Deinococcus RadioduransProtein crystallography data
The structure of Crystal Structure of M1 Zinc Metallopeptidase From Deinococcus Radiodurans, PDB code: 6a8z
was solved by
R.Agrawal,
A.Kumar,
R.D.Makde,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6a8z:
The structure of Crystal Structure of M1 Zinc Metallopeptidase From Deinococcus Radiodurans also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of M1 Zinc Metallopeptidase From Deinococcus Radiodurans
(pdb code 6a8z). 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 M1 Zinc Metallopeptidase From Deinococcus Radiodurans, PDB code: 6a8z: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 6a8zGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the Crystal Structure of M1 Zinc Metallopeptidase From Deinococcus Radiodurans
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 6a8zGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the Crystal Structure of M1 Zinc Metallopeptidase From Deinococcus Radiodurans
![]() Mono view ![]() Stereo pair view
Reference:
R.Agrawal,
V.D.Goyal,
A.Kumar,
N.K.Gaur,
S.N.Jamdar,
A.Kumar,
R.D.Makde.
Two-Domain Aminopeptidase of M1 Family: Structural Features For Substrate Binding and Gating in Absence of C-Terminal Domain. J.Struct.Biol. V. 208 51 2019.
Page generated: Mon Oct 28 17:26:35 2024
ISSN: ESSN 1095-8657 PubMed: 31351924 DOI: 10.1016/J.JSB.2019.07.010 |
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