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Atomistry » Chlorine » PDB 4hmr-4hvt » 4hql | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4hmr-4hvt » 4hql » |
Chlorine in PDB 4hql: Crystal Structure of Magnesium-Loaded Plasmodium Vivax Trap ProteinProtein crystallography data
The structure of Crystal Structure of Magnesium-Loaded Plasmodium Vivax Trap Protein, PDB code: 4hql
was solved by
G.Song,
A.C.Koksal,
C.Lu,
T.A.Springer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4hql:
The structure of Crystal Structure of Magnesium-Loaded Plasmodium Vivax Trap Protein also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Magnesium-Loaded Plasmodium Vivax Trap Protein
(pdb code 4hql). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Magnesium-Loaded Plasmodium Vivax Trap Protein, PDB code: 4hql: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 4hqlGo back to Chlorine Binding Sites List in 4hql
Chlorine binding site 1 out
of 2 in the Crystal Structure of Magnesium-Loaded Plasmodium Vivax Trap Protein
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 4hqlGo back to Chlorine Binding Sites List in 4hql
Chlorine binding site 2 out
of 2 in the Crystal Structure of Magnesium-Loaded Plasmodium Vivax Trap Protein
Mono view Stereo pair view
Reference:
G.Song,
A.C.Koksal,
C.Lu,
T.A.Springer.
Shape Change in the Receptor For Gliding Motility in Plasmodium Sporozoites. Proc.Natl.Acad.Sci.Usa V. 109 21420 2012.
Page generated: Sat Dec 12 10:43:24 2020
ISSN: ISSN 0027-8424 PubMed: 23236185 DOI: 10.1073/PNAS.1218581109 |
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