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Atomistry » Zinc » PDB 4x3p-4xfw » 4xdo | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4x3p-4xfw » 4xdo » |
Zinc in PDB 4xdo: Crystal Structure of Human KDM4C Catalytic Domain with OgaProtein crystallography data
The structure of Crystal Structure of Human KDM4C Catalytic Domain with Oga, PDB code: 4xdo
was solved by
K.K.Swinger,
P.A.Boriack-Sjodin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4xdo:
The structure of Crystal Structure of Human KDM4C Catalytic Domain with Oga also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human KDM4C Catalytic Domain with Oga
(pdb code 4xdo). 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 Human KDM4C Catalytic Domain with Oga, PDB code: 4xdo: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 4xdoGo back to Zinc Binding Sites List in 4xdo
Zinc binding site 1 out
of 2 in the Crystal Structure of Human KDM4C Catalytic Domain with Oga
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 4xdoGo back to Zinc Binding Sites List in 4xdo
Zinc binding site 2 out
of 2 in the Crystal Structure of Human KDM4C Catalytic Domain with Oga
Mono view Stereo pair view
Reference:
T.J.Wigle,
K.K.Swinger,
J.E.Campbell,
M.D.Scholle,
J.Sherrill,
E.A.Admirand,
P.A.Boriack-Sjodin,
K.W.Kuntz,
R.Chesworth,
M.P.Moyer,
M.P.Scott,
R.A.Copeland.
A High-Throughput Mass Spectrometry Assay Coupled with Redox Activity Testing Reduces Artifacts and False Positives in Lysine Demethylase Screening. J Biomol Screen 2015.
Page generated: Sun Oct 27 10:30:41 2024
ISSN: ESSN 1552-454X PubMed: 25755264 DOI: 10.1177/1087057115575689 |
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