tóng-àn:Serpin mechanism.png
Seng khoàⁿ chiàm-liōng: 725 × 599 siōng-sò͘. Kî-thaⁿ--ê kái-sek-tō͘: 290 × 240 siōng-sò͘ | 581 × 480 siōng-sò͘ | 929 × 768 siōng-sò͘ | 1,239 × 1,024 siōng-sò͘ | 1,800 × 1,488 siōng-sò͘.
Choân kái-sek-tō͘ （1,800 × 1,488 siōng-sò͘ , tóng-àn chiàm-liōng: 513 KB, MIME luī-hêng: image/png）
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Khài-iàu
| Soat-bêng |
English: Serine proteases operate by a two-step catalytic mechanism. First, the substrate (blue) is attacked by the catalytic triad (red) to form an acyl-enzyme intermediate. The intermediate is typically resolved by hydrolysis by water. However, when the reactive centre loop (RCL) of a serpin is attacked, the conformational change (blue arrow) pulls the catalytic triad out of position, preventing it from completing catalysis. (Based on PDB: 1K9O, 1EZX) |
| Ji̍t-kî | |
| Chhut-chhù | Ka-tī chò--ê |
| Chok-chiá | Thomas Shafee |
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Tóng-àn le̍k-sú
Chhi̍h ji̍t-kî/sî-kan, khoàⁿ hit sî-chūn--ê tóng-àn.
| Ji̍t-kî/Sî-kan | 細張圖 | 寸尺 | Iōng-chiá | Chù-kái | |
|---|---|---|---|---|---|
| hiān-chāi | 2015-nî 12-goe̍h 22-ji̍t (pài-jī) 09:56 | | 1,800 × 1,488（513 KB） | Evolution and evolvability | Higher resolution |
| 2015-nî 12-goe̍h 19-ji̍t (pài-la̍k) 05:19 |  | 1,362 × 1,126（300 KB） | Evolution and evolvability | Minor arrow correction | |
| 2015-nî 12-goe̍h 19-ji̍t (pài-la̍k) 05:08 |  | 1,362 × 1,126（300 KB） | Evolution and evolvability | added arrow and removed transparency | |
| 2015-nî 12-goe̍h 19-ji̍t (pài-la̍k) 05:04 |  | 1,362 × 1,114（360 KB） | Evolution and evolvability | Cross-wiki upload from en.wikipedia.org |
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