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Atomistry » Sodium » PDB 5m1e-5mfr » 5mc2 » |
Sodium in PDB 5mc2: Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro LigandEnzymatic activity of Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand
All present enzymatic activity of Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand:
3.4.13.9; Protein crystallography data
The structure of Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand, PDB code: 5mc2
was solved by
P.Wilk,
U.Mueller,
H.Dobbek,
M.S.Weiss,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5mc2:
The structure of Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand
(pdb code 5mc2). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand, PDB code: 5mc2: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 5mc2Go back to Sodium Binding Sites List in 5mc2
Sodium binding site 1 out
of 2 in the Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 5mc2Go back to Sodium Binding Sites List in 5mc2
Sodium binding site 2 out
of 2 in the Crystal Structure of GLY278ASP Mutant of Human Prolidase with Mn Ions and Glypro Ligand
Mono view Stereo pair view
Reference:
P.Wilk,
M.Uehlein,
R.Piwowarczyk,
H.Dobbek,
U.Mueller,
M.S.Weiss.
Structural Basis For Prolidase Deficiency Disease Mechanisms. Febs J. V. 285 3422 2018.
Page generated: Tue Dec 15 11:17:19 2020
ISSN: ISSN 1742-4658 PubMed: 30066404 DOI: 10.1111/FEBS.14620 |
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