1kth
From Proteopedia
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|PDB= 1kth |SIZE=350|CAPTION= <scene name='initialview01'>1kth</scene>, resolution 0.95Å | |PDB= 1kth |SIZE=350|CAPTION= <scene name='initialview01'>1kth</scene>, resolution 0.95Å | ||
|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=[[2knt|2KNT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kth OCA], [http://www.ebi.ac.uk/pdbsum/1kth PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kth RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure. | The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure. | ||
| - | |||
| - | ==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: Prange, T.]] | [[Category: Prange, T.]] | ||
| - | [[Category: PO4]] | ||
[[Category: anisotropic refinement]] | [[Category: anisotropic refinement]] | ||
[[Category: connective tissue]] | [[Category: connective tissue]] | ||
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[[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 Sun Mar 30 21:53:21 2008'' |
Revision as of 18:53, 30 March 2008
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| , resolution 0.95Å | |||||||
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| Ligands: | |||||||
| Related: | 2KNT
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom
Overview
The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure.
About this Structure
1KTH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A)., Arnoux B, Ducruix A, Prange T, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1252-4. Epub 2002, Jun 20. PMID:12077460
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