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Atomistry » Chlorine » PDB 4ykx-4yvf » 4ytg » |
Chlorine 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:
Chlorine Binding Sites:
The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Porphyromonas Gingivalis Peptidylarginine Deiminase (Ppad) Mutant C351A in Complex with Dipeptide Met-Arg., PDB code: 4ytg: Chlorine binding site 1 out of 1 in 4ytgGo back to![]() ![]()
Chlorine 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: Sat Dec 12 11:26:21 2020
ISSN: ESSN 2045-2322 PubMed: 26132828 DOI: 10.1038/SREP11969 |
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