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Magnesium in PDB 4v07: Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution

Enzymatic activity of Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution

All present enzymatic activity of Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution:
3.4.21.97;

Protein crystallography data

The structure of Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution, PDB code: 4v07 was solved by M.Zuehlsdorf, S.Werten, G.J.Palm, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.66 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.375, 75.986, 110.758, 90.00, 90.00, 90.00
R / Rfree (%) 17.788 / 23.732

Other elements in 4v07:

The structure of Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution also contains other interesting chemical elements:

Chlorine (Cl) 7 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution (pdb code 4v07). 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 Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution, PDB code: 4v07:

Magnesium binding site 1 out of 1 in 4v07

Go back to Magnesium Binding Sites List in 4v07
Magnesium binding site 1 out of 1 in the Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dimeric Pseudorabies Virus Protease PUL26N at 2.1 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1223

b:75.7
occ:1.00
O A:HOH2034 1.8 72.6 1.0
O A:HOH2063 1.9 54.8 1.0
O A:HOH2033 1.9 59.6 1.0
O A:HOH2064 2.1 65.6 1.0
O A:HOH2032 2.6 56.1 1.0
OD2 A:ASP145 3.6 40.4 1.0
OD1 A:ASP145 4.1 35.7 1.0
CG A:ASP145 4.3 38.4 1.0
O A:HOH2031 4.9 54.5 1.0

Reference:

M.Zuehlsdorf, S.Werten, B.G.Klupp, G.J.Palm, T.Mettenleiter, W.Hinrichs. Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin PUL26N, A Herpesvirus Serine Protease Plos Pathog. V. 11 5045 2015.
ISSN: ISSN 1553-7366
PubMed: 26161660
DOI: 10.1371/JOURNAL.PPAT.1005045
Page generated: Tue Aug 20 05:02:29 2024

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