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Atomistry » Nickel » PDB 2gw4-2pos » 2oq6 » |
Nickel 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:
Nickel Binding Sites:
The binding sites of Nickel 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 Nickel atom.
In total 2 binding sites of Nickel where determined in the Crystal Structure of JMJD2A Complexed with Histone H3 Peptide Trimethylated at LYS9, PDB code: 2oq6: Jump to Nickel binding site number: 1; 2; Nickel binding site 1 out of 2 in 2oq6Go back to Nickel Binding Sites List in 2oq6
Nickel 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
Nickel binding site 2 out of 2 in 2oq6Go back to Nickel Binding Sites List in 2oq6
Nickel 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: Wed Dec 16 01:19:08 2020
ISSN: ISSN 0028-0836 PubMed: 17589501 DOI: 10.1038/NATURE05971 |
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