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Atomistry » Calcium » PDB 5wzv-5xiw » 5x9s | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5wzv-5xiw » 5x9s » |
Calcium in PDB 5x9s: Crystal Structure of Fully Modified H-Ras-GppnhpProtein crystallography data
The structure of Crystal Structure of Fully Modified H-Ras-Gppnhp, PDB code: 5x9s
was solved by
S.Matsumoto,
H.Ke,
Y.Murashima,
H.Taniguchi-Tamura,
R.Miyamoto,
Y.Yoshikawa,
T.Kumasaka,
E.Mizohata,
H.Edamatsu,
T.Kataoka,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5x9s:
The structure of Crystal Structure of Fully Modified H-Ras-Gppnhp also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Fully Modified H-Ras-Gppnhp
(pdb code 5x9s). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Fully Modified H-Ras-Gppnhp, PDB code: 5x9s: Jump to Calcium binding site number: 1; 2; 3; Calcium binding site 1 out of 3 in 5x9sGo back to Calcium Binding Sites List in 5x9s
Calcium binding site 1 out
of 3 in the Crystal Structure of Fully Modified H-Ras-Gppnhp
Mono view Stereo pair view
Calcium binding site 2 out of 3 in 5x9sGo back to Calcium Binding Sites List in 5x9s
Calcium binding site 2 out
of 3 in the Crystal Structure of Fully Modified H-Ras-Gppnhp
Mono view Stereo pair view
Calcium binding site 3 out of 3 in 5x9sGo back to Calcium Binding Sites List in 5x9s
Calcium binding site 3 out
of 3 in the Crystal Structure of Fully Modified H-Ras-Gppnhp
Mono view Stereo pair view
Reference:
H.Ke,
S.Matsumoto,
Y.Murashima,
H.Taniguchi-Tamura,
R.Miyamoto,
Y.Yoshikawa,
C.Tsuda,
T.Kumasaka,
E.Mizohata,
H.Edamatsu,
T.Kataoka.
Structural Basis For Intramolecular Interaction of Post-Translationally Modified H-Rasgtp Prepared By Protein Ligation Febs Lett. V. 591 2470 2017.
Page generated: Mon Jul 15 14:51:22 2024
ISSN: ISSN 1873-3468 PubMed: 28730604 DOI: 10.1002/1873-3468.12759 |
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