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Atomistry » Zinc » PDB 3v2m-3vh1 » 3v6e | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3v2m-3vh1 » 3v6e » |
Zinc in PDB 3v6e: Crystal Structure of USP2 and A Mutant Form of UbiquitinEnzymatic activity of Crystal Structure of USP2 and A Mutant Form of Ubiquitin
All present enzymatic activity of Crystal Structure of USP2 and A Mutant Form of Ubiquitin:
3.4.19.12; Protein crystallography data
The structure of Crystal Structure of USP2 and A Mutant Form of Ubiquitin, PDB code: 3v6e
was solved by
M.Neculai,
A.Ernst,
S.Sidhu,
C.H.Arrowsmith,
A.M.Edwards,
C.Bountra,
J.Weigelt,
S.Dhe-Paganon,
Structural Genomics Consortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3v6e:
The structure of Crystal Structure of USP2 and A Mutant Form of Ubiquitin also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of USP2 and A Mutant Form of Ubiquitin
(pdb code 3v6e). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of USP2 and A Mutant Form of Ubiquitin, PDB code: 3v6e: Zinc binding site 1 out of 1 in 3v6eGo back to Zinc Binding Sites List in 3v6e
Zinc binding site 1 out
of 1 in the Crystal Structure of USP2 and A Mutant Form of Ubiquitin
Mono view Stereo pair view
Reference:
A.Ernst,
G.Avvakumov,
J.Tong,
Y.Fan,
Y.Zhao,
P.Alberts,
A.Persaud,
J.R.Walker,
A.M.Neculai,
D.Neculai,
A.Vorobyov,
P.Garg,
L.Beatty,
P.K.Chan,
Y.C.Juang,
M.C.Landry,
C.Yeh,
E.Zeqiraj,
K.Karamboulas,
A.Allali-Hassani,
M.Vedadi,
M.Tyers,
J.Moffat,
F.Sicheri,
L.Pelletier,
D.Durocher,
B.Raught,
D.Rotin,
J.Yang,
M.F.Moran,
S.Dhe-Paganon,
S.S.Sidhu.
A Strategy For Modulation of Enzymes in the Ubiquitin System. Science V. 339 590 2013.
Page generated: Wed Dec 16 04:55:43 2020
ISSN: ISSN 0036-8075 PubMed: 23287719 DOI: 10.1126/SCIENCE.1230161 |
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