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Atomistry » Sodium » PDB 4yil-4z48 » 4ytg » |
Sodium in PDB 4ytg: Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase (Ppad) Mutant C351A in Complex with Dipeptide Met-Arg.Protein crystallography data
The structure of Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase (Ppad) Mutant C351A in Complex with Dipeptide Met-Arg., PDB code: 4ytg
was solved by
T.Goulas,
D.Mizgalska,
I.Garcia-Ferrer,
T.Kantyka,
T.Guevara,
B.Szmigielski,
A.Sroka,
C.Millan,
I.Uson,
F.Veillard,
B.Potempa,
P.Mydel,
M.Sola,
J.Potempa,
F.X.Gomis-Ruth,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4ytg:
The structure of Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase (Ppad) Mutant C351A in Complex with Dipeptide Met-Arg. also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase (Ppad) Mutant C351A in Complex with Dipeptide Met-Arg.
(pdb code 4ytg). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase (Ppad) Mutant C351A in Complex with Dipeptide Met-Arg., PDB code: 4ytg: Sodium binding site 1 out of 1 in 4ytgGo back to![]() ![]()
Sodium binding site 1 out
of 1 in the Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase (Ppad) Mutant C351A in Complex with Dipeptide Met-Arg.
![]() Mono view ![]() Stereo pair view
Reference:
T.Goulas,
D.Mizgalska,
I.Garcia-Ferrer,
T.Kantyka,
T.Guevara,
B.Szmigielski,
A.Sroka,
C.Millan,
I.Uson,
F.Veillard,
B.Potempa,
P.Mydel,
M.Sola,
J.Potempa,
F.X.Gomis-Ruth.
Structure and Mechanism of A Bacterial Host-Protein Citrullinating Virulence Factor, Porphyromonas Gingivalis Peptidylarginine Deiminase. Sci Rep V. 5 11969 2015.
Page generated: Mon Oct 7 19:34:40 2024
ISSN: ESSN 2045-2322 PubMed: 26132828 DOI: 10.1038/SREP11969 |
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