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Atomistry » Sodium » PDB 3ogc-3p1l » 3oyo | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 3ogc-3p1l » 3oyo » |
Sodium in PDB 3oyo: Crystal Structure of Hemopexin Fold Protein CP4 From Cow PeaProtein crystallography data
The structure of Crystal Structure of Hemopexin Fold Protein CP4 From Cow Pea, PDB code: 3oyo
was solved by
V.Gaur,
V.Chanana,
D.M.Salunke,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3oyo:
The structure of Crystal Structure of Hemopexin Fold Protein CP4 From Cow Pea also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Hemopexin Fold Protein CP4 From Cow Pea
(pdb code 3oyo). 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 Hemopexin Fold Protein CP4 From Cow Pea, PDB code: 3oyo: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 3oyoGo back to![]() ![]()
Sodium binding site 1 out
of 2 in the Crystal Structure of Hemopexin Fold Protein CP4 From Cow Pea
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 3oyoGo back to![]() ![]()
Sodium binding site 2 out
of 2 in the Crystal Structure of Hemopexin Fold Protein CP4 From Cow Pea
![]() Mono view ![]() Stereo pair view
Reference:
V.Gaur,
V.Chanana,
A.Jain,
D.M.Salunke.
The Structure of A Haemopexin-Fold Protein From Cow Pea (Vigna Unguiculata) Suggests Functional Diversity of Haemopexins in Plants Acta Crystallogr.,Sect.F V. 67 193 2011.
Page generated: Mon Oct 7 12:07:42 2024
ISSN: ESSN 1744-3091 PubMed: 21301085 DOI: 10.1107/S1744309110051250 |
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