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Magnesium in PDB 8dy8: Crystal Structure of the R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1)

Enzymatic activity of Crystal Structure of the R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1)

All present enzymatic activity of Crystal Structure of the R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1):
3.4.19.12;

Protein crystallography data

The structure of Crystal Structure of the R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1), PDB code: 8dy8 was solved by S.Kenny, K.J.Brown, C.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.92 / 2.10
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 109.385, 109.385, 79.202, 90, 90, 90
R / Rfree (%) 22.2 / 26.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1) (pdb code 8dy8). 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 R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1), PDB code: 8dy8:

Magnesium binding site 1 out of 1 in 8dy8

Go back to Magnesium Binding Sites List in 8dy8
Magnesium binding site 1 out of 1 in the Crystal Structure of the R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1)


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 R178Q Mutant of Ubiquitin Carboxy Terminal Hydrolase L1 (Uch-L1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg302

b:63.2
occ:1.00
 N B:ASP169 3.2 67.4 1.0
CA B:ASP169 3.7 71.7 1.0
CB B:ASP169 4.3 74.8 1.0
C B:VAL168 4.3 63.0 1.0
CA B:VAL168 4.5 59.8 1.0
CD B:LYS78 4.7 74.7 1.0
CG1 B:VAL168 4.7 60.0 1.0
OD1 B:ASP169 4.8 91.3 1.0

Reference:

S.Kenny, K.J.Brown, C.Das. Enhanced Catalytic Activity of the UCHL1R178Q Mutant Is Due to A More Reactive Active Site To Be Published.
Page generated: Fri Oct 4 00:58:34 2024

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