2ill
From Proteopedia
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| - | [[Image:2ill.jpg|left|200px]] | + | [[Image:2ill.jpg|left|200px]] |
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| - | '''Anomalous substructure of Titin-A168169''' | + | {{Structure |
| + | |PDB= 2ill |SIZE=350|CAPTION= <scene name='initialview01'>2ill</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Anomalous substructure of Titin-A168169''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ILL is a [ | + | 2ILL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILL OCA]. |
==Reference== | ==Reference== | ||
| - | On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths., Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:[http:// | + | On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths., Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17327674 17327674] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
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[[Category: long wavelength]] | [[Category: long wavelength]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:30:53 2008'' |
Revision as of 15:30, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Anomalous substructure of Titin-A168169
Contents |
Overview
23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.
Disease
Known diseases associated with this structure: Cardiomyopathy, dilated, 1G OMIM:[188840], Cardiomyopathy, familial hypertrophic OMIM:[188840], Muscular dystrophy, limb-girdle, type 2J OMIM:[188840], Myopathy, early-onset, with fatal cardiomyopathy OMIM:[188840], Myopathy, proximal, with early respiratory muscle involvement OMIM:[188840], Tibial muscular dystrophy, tardive OMIM:[188840]
About this Structure
2ILL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths., Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674
Page seeded by OCA on Thu Mar 20 17:30:53 2008
