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Atomistry » Iron » PDB 4x3s-4xq1 » 4xdp | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 4x3s-4xq1 » 4xdp » |
Iron in PDB 4xdp: Crystal Structure of Human KDM4C Catalytic Domain Bound to TrisProtein crystallography data
The structure of Crystal Structure of Human KDM4C Catalytic Domain Bound to Tris, PDB code: 4xdp
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 4xdp:
The structure of Crystal Structure of Human KDM4C Catalytic Domain Bound to Tris also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Human KDM4C Catalytic Domain Bound to Tris
(pdb code 4xdp). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Human KDM4C Catalytic Domain Bound to Tris, PDB code: 4xdp: Jump to Iron binding site number: 1; 2; Iron binding site 1 out of 2 in 4xdpGo back to Iron Binding Sites List in 4xdp
Iron binding site 1 out
of 2 in the Crystal Structure of Human KDM4C Catalytic Domain Bound to Tris
Mono view Stereo pair view
Iron binding site 2 out of 2 in 4xdpGo back to Iron Binding Sites List in 4xdp
Iron binding site 2 out
of 2 in the Crystal Structure of Human KDM4C Catalytic Domain Bound to Tris
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 Dec 13 15:51:47 2020
ISSN: ESSN 1552-454X PubMed: 25755264 DOI: 10.1177/1087057115575689 |
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