1KTH

The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom

1KTH の概要

• エントリーDOI: 10.2210/pdb1kth/pdb
• 関連するPDBエントリー: 2KNT
• 分子名称: Collagen alpha 3(VI) chain, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: anisotropic refinement, kunitz inhibitor, extracellular matrix, connective tissue, structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix : P12111
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6829.45

構造登録者

Arnoux, B.,Ducruix, A.,Prange, T. (登録日: 2002-01-16, 公開日: 2002-02-06, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (0.95 Å)