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Zinc in PDB 7v8g: Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr DomainEnzymatic activity of Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain
All present enzymatic activity of Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain:
2.3.2.27; 2.3.2.31; Protein crystallography data
The structure of Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain, PDB code: 7v8g
was solved by
J.Liu,
Y.Wang,
L.Pan,
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 Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain
(pdb code 7v8g). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain, PDB code: 7v8g: Jump to Zinc binding site number: 1; 2; 3; 4; Zinc binding site 1 out of 4 in 7v8gGo back to Zinc Binding Sites List in 7v8g
Zinc binding site 1 out
of 4 in the Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain
Mono view Stereo pair view
Zinc binding site 2 out of 4 in 7v8gGo back to Zinc Binding Sites List in 7v8g
Zinc binding site 2 out
of 4 in the Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain
Mono view Stereo pair view
Zinc binding site 3 out of 4 in 7v8gGo back to Zinc Binding Sites List in 7v8g
Zinc binding site 3 out
of 4 in the Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain
Mono view Stereo pair view
Zinc binding site 4 out of 4 in 7v8gGo back to Zinc Binding Sites List in 7v8g
Zinc binding site 4 out
of 4 in the Crystal Structure of Hoip RING1 Domain Bound to IPAH1.4 Lrr Domain
Mono view Stereo pair view
Reference:
J.Liu,
Y.Wang,
D.Wang,
Y.Wang,
X.Xu,
Y.Zhang,
Y.Li,
M.Zhang,
X.Gong,
Y.Tang,
L.Shen,
M.Li,
L.Pan.
Mechanistic Insights Into the Subversion of the Linear Ubiquitin Chain Assembly Complex By the E3 Ligase IPAH1.4 of Shigella Flexneri. Proc.Natl.Acad.Sci.Usa V. 119 76119 2022.
Page generated: Wed Oct 30 12:35:00 2024
ISSN: ESSN 1091-6490 PubMed: 35294289 DOI: 10.1073/PNAS.2116776119 |
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