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Atomistry » Zinc » PDB 1ml9-1my1 » 1ml9 » |
Zinc in PDB 1ml9: Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine MethyltransferaseEnzymatic activity of Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase
All present enzymatic activity of Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase:
2.1.1.43; Protein crystallography data
The structure of Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase, PDB code: 1ml9
was solved by
X.Zhang,
H.Tamaru,
S.I.Khan,
J.R.Horton,
L.J.Keefe,
E.U.Selker,
X.Cheng,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase
(pdb code 1ml9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase, PDB code: 1ml9: Jump to Zinc binding site number: 1; 2; 3; Zinc binding site 1 out of 3 in 1ml9Go back to![]() ![]()
Zinc binding site 1 out
of 3 in the Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 3 in 1ml9Go back to![]() ![]()
Zinc binding site 2 out
of 3 in the Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase
![]() Mono view ![]() Stereo pair view
Zinc binding site 3 out of 3 in 1ml9Go back to![]() ![]()
Zinc binding site 3 out
of 3 in the Structure of the Neurospora Set Domain Protein Dim-5, A Histone Lysine Methyltransferase
![]() Mono view ![]() Stereo pair view
Reference:
X.Zhang,
H.Tamaru,
S.I.Khan,
J.R.Horton,
L.J.Keefe,
E.U.Selker,
X.Cheng.
Structure of the Neurospora Set Domain Protein Dim-5, A Histone H3 Lysine Methyltransferase Cell(Cambridge,Mass.) V. 111 117 2002.
Page generated: Wed Oct 16 16:59:02 2024
ISSN: ISSN 0092-8674 PubMed: 12372305 DOI: 10.1016/S0092-8674(02)00999-6 |
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