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Magnesium in PDB 3rii: Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme

Enzymatic activity of Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme

All present enzymatic activity of Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme:
3.4.19.12;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme, PDB code: 3rii was solved by C.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.05 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.395, 99.034, 48.145, 90.00, 96.39, 90.00
R / Rfree (%) 17.5 / 22.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme (pdb code 3rii). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme, PDB code: 3rii:

Magnesium binding site 1 out of 1 in 3rii

Go back to Magnesium Binding Sites List in 3rii
Magnesium binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome- Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg230

b:71.4
occ:1.00
 OE2 A:GLU109 2.6 61.9 1.0
O A:HOH349 2.6 49.6 1.0
OE2 A:GLU113 2.7 41.8 1.0
OE1 A:GLU113 3.3 42.1 1.0
O A:HOH328 3.4 48.1 1.0
CD A:GLU113 3.4 40.2 1.0
CD A:GLU109 3.6 59.9 1.0
CG A:GLU109 4.0 46.3 1.0
OE1 A:GLU109 4.6 64.1 1.0
O A:HOH263 4.7 37.9 1.0
CG A:GLU113 4.8 36.9 1.0
O A:HOH299 5.0 31.9 1.0

Reference:

T.K.Maiti, M.Permaul, D.A.Boudreaux, C.Mahanic, S.Mauney, C.Das. Crystal Structure of the Catalytic Domain of UCHL5, A Proteasome-Associated Human Deubiquitinating Enzyme, Reveals An Unproductive Form of the Enzyme. Febs J. V. 278 4917 2011.
ISSN: ISSN 1742-464X
PubMed: 21995438
DOI: 10.1111/J.1742-4658.2011.08393.X
Page generated: Thu Aug 15 10:29:32 2024

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