1KTH

The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom

Summary for 1KTH

• Entry DOI: 10.2210/pdb1kth/pdb
• Related: 2KNT
• Descriptor: Collagen alpha 3(VI) chain, PHOSPHATE ION (3 entities in total)
• Functional Keywords: anisotropic refinement, kunitz inhibitor, extracellular matrix, connective tissue, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix : P12111
• Total number of polymer chains: 1
• Total formula weight: 6829.45

Authors

Arnoux, B.,Ducruix, A.,Prange, T. (deposition date: 2002-01-16, release date: 2002-02-06, Last modification date: 2024-10-30)

Primary citation

Arnoux, B.,Ducruix, A.,Prange, T.
Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A).
Acta Crystallogr.,Sect.D, 58:1252-1254, 2002

PubMed Abstract: 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.

PubMed: 12077460
DOI: 10.1107/S0907444902007333

Experimental method

X-RAY DIFFRACTION (0.95 Å)