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Magnesium in PDB 4izj: Crystal Structure of Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes.

Enzymatic activity of Crystal Structure of Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes.

All present enzymatic activity of Crystal Structure of Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes.:
3.4.21.115;

Protein crystallography data

The structure of Crystal Structure of Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes., PDB code: 4izj was solved by M.Paetzel, I.Y.W.Chung, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.30 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.610, 64.330, 187.740, 90.00, 95.80, 90.00
R / Rfree (%) 17.8 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes. (pdb code 4izj). 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 Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes., PDB code: 4izj:

Magnesium binding site 1 out of 1 in 4izj

Go back to Magnesium Binding Sites List in 4izj
Magnesium binding site 1 out of 1 in the Crystal Structure of Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes.


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 Yellowtail Ascites Virus VP4 Protease with A Wild-Type Active Site Reveals Acyl-Enzyme Complexes and Product Complexes. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg802

b:33.2
occ:1.00
O A:HOH907 2.2 16.7 1.0
O A:HOH940 2.2 25.4 1.0
OD2 A:ASP602 2.7 38.9 1.0
CG A:ASP602 3.4 40.5 1.0
OD1 A:ASP602 3.8 42.1 1.0
CB A:ASP602 4.5 36.8 1.0
O A:HOH942 4.7 27.7 1.0

Reference:

I.Y.Chung, M.Paetzel. Crystal Structures of Yellowtail Ascites Virus VP4 Protease: Trapping An Internal Cleavage Site Trans Acyl-Enzyme Complex in A Native Ser/Lys Dyad Active Site. J.Biol.Chem. V. 288 13068 2013.
ISSN: ISSN 0021-9258
PubMed: 23511637
DOI: 10.1074/JBC.M112.386953
Page generated: Mon Aug 11 14:30:05 2025

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