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Atomistry » Zinc » PDB 3ax1-3b7i » 3b0a | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3ax1-3b7i » 3b0a » |
Zinc in PDB 3b0a: Crystal Structure of the Mouse HOIL1-L-Nzf in Complex with Linear Di- UbiquitinProtein crystallography data
The structure of Crystal Structure of the Mouse HOIL1-L-Nzf in Complex with Linear Di- Ubiquitin, PDB code: 3b0a
was solved by
Y.Sato,
H.Fujita,
A.Yoshikawa,
M.Yamashita,
A.Yamagata,
S.E.Kaiser,
K.Iwai,
S.Fukai,
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 the Mouse HOIL1-L-Nzf in Complex with Linear Di- Ubiquitin
(pdb code 3b0a). 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 the Mouse HOIL1-L-Nzf in Complex with Linear Di- Ubiquitin, PDB code: 3b0a: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 3b0aGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the Crystal Structure of the Mouse HOIL1-L-Nzf in Complex with Linear Di- Ubiquitin
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 3b0aGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the Crystal Structure of the Mouse HOIL1-L-Nzf in Complex with Linear Di- Ubiquitin
![]() Mono view ![]() Stereo pair view
Reference:
Y.Sato,
H.Fujita,
A.Yoshikawa,
M.Yamashita,
A.Yamagata,
S.E.Kaiser,
K.Iwai,
S.Fukai.
Specific Recognition of Linear Ubiquitin Chains By the NPL4 Zinc Finger (Nzf) Domain of the Hoil-1L Subunit of the Linear Ubiquitin Chain Assembly Complex Proc.Natl.Acad.Sci.Usa V. 108 20520 2011.
Page generated: Thu Oct 24 11:20:35 2024
ISSN: ISSN 0027-8424 PubMed: 22139374 DOI: 10.1073/PNAS.1109088108 |
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