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Atomistry » Manganese » PDB 4nxz-4phd » 4ogc | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 4nxz-4phd » 4ogc » |
Manganese in PDB 4ogc: Crystal Structure of the Type II-C CAS9 Enzyme From Actinomyces NaeslundiiProtein crystallography data
The structure of Crystal Structure of the Type II-C CAS9 Enzyme From Actinomyces Naeslundii, PDB code: 4ogc
was solved by
F.Jiang,
E.Ma,
S.Lin,
J.A.Doudna,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4ogc:
The structure of Crystal Structure of the Type II-C CAS9 Enzyme From Actinomyces Naeslundii also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of the Type II-C CAS9 Enzyme From Actinomyces Naeslundii
(pdb code 4ogc). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Type II-C CAS9 Enzyme From Actinomyces Naeslundii, PDB code: 4ogc: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 4ogcGo back to![]() ![]()
Manganese binding site 1 out
of 2 in the Crystal Structure of the Type II-C CAS9 Enzyme From Actinomyces Naeslundii
![]() Mono view ![]() Stereo pair view
Manganese binding site 2 out of 2 in 4ogcGo back to![]() ![]()
Manganese binding site 2 out
of 2 in the Crystal Structure of the Type II-C CAS9 Enzyme From Actinomyces Naeslundii
![]() Mono view ![]() Stereo pair view
Reference:
M.Jinek,
F.Jiang,
D.W.Taylor,
S.H.Sternberg,
E.Kaya,
E.Ma,
C.Anders,
M.Hauer,
K.Zhou,
S.Lin,
M.Kaplan,
A.T.Iavarone,
E.Charpentier,
E.Nogales,
J.A.Doudna.
Structures of CAS9 Endonucleases Reveal Rna-Mediated Conformational Activation. Science V. 343 47997 2014.
Page generated: Tue Dec 15 04:25:46 2020
ISSN: ISSN 0036-8075 PubMed: 24505130 DOI: 10.1126/SCIENCE.1247997 |
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