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Atomistry » Magnesium » PDB 4ix3-4j99 » 4izj | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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:
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 4izjGo 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
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.
Page generated: Fri Aug 16 17:06:16 2024
ISSN: ISSN 0021-9258 PubMed: 23511637 DOI: 10.1074/JBC.M112.386953 |
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