2HLC
HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION
2HLC の概要
| エントリーDOI | 10.2210/pdb2hlc/pdb |
| 分子名称 | COLLAGENASE (2 entities in total) |
| 機能のキーワード | serine protease, hydrolase, collagen degradation |
| 由来する生物種 | Hypoderma lineatum (early cattle grub) |
| 細胞内の位置 | Secreted: P08897 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 50494.38 |
| 構造登録者 | Broutin, I.,Merigeau, K.,Arnoux, B.,Ducruix, A. (登録日: 1997-01-08, 公開日: 1997-09-04, 最終更新日: 2025-11-12) |
| 主引用文献 | Broutin-L'Hermite, I.,Ries-Kautt, M.,Ducruix, A. 1.7 A x-ray structure of space-grown collagenase crystals. Acta Crystallogr.,Sect.D, 56:376-378, 2000 Cited by PubMed Abstract: Collagenases, divided into metallocollagenases and serine collagenases, are the only proteases that cleave the triple helix of collagen under physiological conditions. In the present work, the serine protease collagenase purified from Hypoderma lineatum larvae is studied. From crystals grown in the International Microgravity Laboratory (IML2), a data set was collected at 1.7 A using synchrotron radiation. Although the resolution is not very different, the signal-to-noise ratio and the quality of the electron density are much improved. Alternate conformations were revealed for several residues, in particular Tyr99, suggesting a gate mechanism of recognition. PubMed: 10713532DOI: 10.1107/s0907444999016789 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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