2knt
From Proteopedia
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|PDB= 2knt |SIZE=350|CAPTION= <scene name='initialview01'>2knt</scene>, resolution 1.20Å | |PDB= 2knt |SIZE=350|CAPTION= <scene name='initialview01'>2knt</scene>, resolution 1.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2knt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2knt OCA], [http://www.ebi.ac.uk/pdbsum/2knt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2knt RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure. | The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Bethlem myopathy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120250 120250]], Ullrich congenital muscular dystrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120250 120250]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Ducruix, A.]] | [[Category: Ducruix, A.]] | ||
[[Category: Merigeau, K.]] | [[Category: Merigeau, K.]] | ||
| - | [[Category: PO4]] | ||
[[Category: connective tissue]] | [[Category: connective tissue]] | ||
[[Category: extracellular matrix]] | [[Category: extracellular matrix]] | ||
[[Category: kunitz inhibitor]] | [[Category: kunitz inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:03:07 2008'' |
Revision as of 01:03, 31 March 2008
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| , resolution 1.20Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5
Overview
The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.
About this Structure
2KNT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
1.2 A refinement of the Kunitz-type domain from the alpha3 chain of human type VI collagen., Merigeau K, Arnoux B, Perahia D, Norris K, Norris F, Ducruix A, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):306-12. PMID:9761897
Page seeded by OCA on Mon Mar 31 04:03:07 2008
