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Atomistry » Zinc » PDB 2pop-2q1q » 2pxj | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2pop-2q1q » 2pxj » |
Zinc in PDB 2pxj: The Complex Structure of JMJD2A and Monomethylated H3K36 PeptideProtein crystallography data
The structure of The Complex Structure of JMJD2A and Monomethylated H3K36 Peptide, PDB code: 2pxj
was solved by
Z.Chen,
J.Zang,
J.Kappler,
X.Hong,
F.Crawford,
G.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2pxj:
The structure of The Complex Structure of JMJD2A and Monomethylated H3K36 Peptide also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Complex Structure of JMJD2A and Monomethylated H3K36 Peptide
(pdb code 2pxj). 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 Complex Structure of JMJD2A and Monomethylated H3K36 Peptide, PDB code: 2pxj: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2pxjGo back to Zinc Binding Sites List in 2pxj
Zinc binding site 1 out
of 2 in the The Complex Structure of JMJD2A and Monomethylated H3K36 Peptide
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2pxjGo back to Zinc Binding Sites List in 2pxj
Zinc binding site 2 out
of 2 in the The Complex Structure of JMJD2A and Monomethylated H3K36 Peptide
Mono view Stereo pair view
Reference:
Z.Chen,
J.Zang,
J.Kappler,
X.Hong,
F.Crawford,
Q.Wang,
F.Lan,
C.Jiang,
J.Whetstine,
S.Dai,
K.Hansen,
Y.Shi,
G.Zhang.
Structural Basis of the Recognition of A Methylated Histone Tail By JMJD2A Proc.Natl.Acad.Sci.Usa V. 104 10818 2007.
Page generated: Wed Dec 16 03:49:24 2020
ISSN: ISSN 0027-8424 PubMed: 17567753 DOI: 10.1073/PNAS.0704525104 |
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