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Atomistry » Magnesium » PDB 3fps-3fzi » 3fqt | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 3fps-3fzi » 3fqt » |
Magnesium in PDB 3fqt: Phosphorylation of Self-Peptides Alters Human Leukocyte Antigen Class I-Restricted Antigen Presentation and Generates Tumor Specific EpitopesProtein crystallography data
The structure of Phosphorylation of Self-Peptides Alters Human Leukocyte Antigen Class I-Restricted Antigen Presentation and Generates Tumor Specific Epitopes, PDB code: 3fqt
was solved by
J.Petersen,
J.Rossjohn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3fqt:
The structure of Phosphorylation of Self-Peptides Alters Human Leukocyte Antigen Class I-Restricted Antigen Presentation and Generates Tumor Specific Epitopes also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Phosphorylation of Self-Peptides Alters Human Leukocyte Antigen Class I-Restricted Antigen Presentation and Generates Tumor Specific Epitopes
(pdb code 3fqt). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Phosphorylation of Self-Peptides Alters Human Leukocyte Antigen Class I-Restricted Antigen Presentation and Generates Tumor Specific Epitopes, PDB code: 3fqt: Magnesium binding site 1 out of 1 in 3fqtGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Phosphorylation of Self-Peptides Alters Human Leukocyte Antigen Class I-Restricted Antigen Presentation and Generates Tumor Specific Epitopes
![]() Mono view ![]() Stereo pair view
Reference:
J.Petersen,
S.J.Wurzbacher,
N.A.Williamson,
S.H.Ramarathinam,
H.H.Reid,
A.K.Nair,
A.Y.Zhao,
R.Nastovska,
G.Rudge,
J.Rossjohn,
A.W.Purcell.
Phosphorylated Self-Peptides Alter Human Leukocyte Antigen Class I-Restricted Antigen Presentation and Generate Tumor-Specific Epitopes Proc.Natl.Acad.Sci.Usa V. 106 2776 2009.
Page generated: Wed Aug 14 13:52:20 2024
ISSN: ISSN 0027-8424 PubMed: 19196958 DOI: 10.1073/PNAS.0812901106 |
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