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Zinc in PDB 6cw2: Crystal Structure of A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1Enzymatic activity of Crystal Structure of A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1
All present enzymatic activity of Crystal Structure of A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1:
2.3.1.48; Protein crystallography data
The structure of Crystal Structure of A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1, PDB code: 6cw2
was solved by
J.Sun,
M.Paduch,
S.A.Kim,
R.M.Kramer,
A.F.Barrios,
V.Lu,
J.Luke,
S.Usatyuk,
A.A.Kossiakoff,
S.Tan,
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 Crystal Structure of A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1
(pdb code 6cw2). 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 A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1, PDB code: 6cw2: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 6cw2Go back to Zinc Binding Sites List in 6cw2
Zinc binding site 1 out
of 2 in the Crystal Structure of A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 6cw2Go back to Zinc Binding Sites List in 6cw2
Zinc binding site 2 out
of 2 in the Crystal Structure of A Yeast Saga Transcriptional Coactivator ADA2/GCN5 Hat Subcomplex, Crystal Form 1
Mono view Stereo pair view
Reference:
J.Sun,
M.Paduch,
S.A.Kim,
R.M.Kramer,
A.F.Barrios,
V.Lu,
J.Luke,
S.Usatyuk,
A.A.Kossiakoff,
S.Tan.
Structural Basis For Activation of Saga Histone Acetyltransferase GCN5 By Partner Subunit ADA2. Proc. Natl. Acad. Sci. V. 115 10010 2018U.S.A..
Page generated: Wed Dec 16 11:38:20 2020
ISSN: ESSN 1091-6490 PubMed: 30224453 DOI: 10.1073/PNAS.1805343115 |
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