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Atomistry » Zinc » PDB 2omg-2ovx » 2oq6 » |
Zinc in PDB 2oq6: Crystal Structure of JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9Protein crystallography data
The structure of Crystal Structure of JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9, PDB code: 2oq6
was solved by
E.S.Pilka,
S.S.Ng,
K.L.Kavanagh,
M.A.Mcdonough,
P.Savitsky,
F.Von Delft,
C.H.Arrowsmith,
J.Weigelt,
A.Edwards,
M.Sundstrom,
C.J.Schofield,
U.Oppermann,
Structural Genomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2oq6:
The structure of Crystal Structure of JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9
(pdb code 2oq6). 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 JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9, PDB code: 2oq6: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2oq6Go back to Zinc Binding Sites List in 2oq6
Zinc binding site 1 out
of 2 in the Crystal Structure of JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2oq6Go back to Zinc Binding Sites List in 2oq6
Zinc binding site 2 out
of 2 in the Crystal Structure of JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9
Mono view Stereo pair view
Reference:
S.S.Ng,
K.L.Kavanagh,
M.A.Mcdonough,
D.Butler,
E.S.Pilka,
B.M.Lienard,
J.E.Bray,
P.Savitsky,
O.Gileadi,
F.Von Delft,
N.R.Rose,
J.Offer,
J.C.Scheinost,
T.Borowski,
M.Sundstrom,
C.J.Schofield,
U.Oppermann.
Crystal Structures of Histone Demethylase JMJD2A Reveal Basis For Substrate Specificity. Nature V. 448 87 2007.
Page generated: Thu Oct 17 02:43:24 2024
ISSN: ISSN 0028-0836 PubMed: 17589501 DOI: 10.1038/NATURE05971 |
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