Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Sept 2011.
Explore 3S9C in 3D Show helices and sheets RCSB PDB PDBe
3S9C contains 7 α-helices and 22 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 3 |
| β-strand | 37-48 | 12 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 81-83 | 3 | 3 |
| β-strand | 85-89 | 5 | 3 |
| α-helix | 99-101 | 3 | |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 4 |
| β-strand | 118 | 1 | 4 |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-124 | 2 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 145 | 1 | 5 |
| β-strand | 148 | 1 | 5 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 165-167 | 3 | |
| β-strand | 180-184 | 5 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-201 | 4 | 2 |
| β-strand | 208-215 | 8 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-243 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1544 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vipera russelli proteinase RVV-V gamma | A | protein | 234 | Daboia russellii siamensis | P18965 (AlphaFold model) |
| Coagulation factor V | B | protein | 14 | Homo sapiens | P12259 (AlphaFold model) |
>3S9C_1 Vipera russelli proteinase RVV-V gamma (chains A) VVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNI RNEDEQIRVPRGKYFCLNTKFPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRC RIMGWGKISTTTYPDVPHCTNIFIVKHKWCEPLYPWVPADSRTLCAGILKGGRDTCHGDS GGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP
>3S9C_2 Coagulation factor V (chains B) SRDPDNIAAWYLRS
Water and common crystallization additives (ACT) are not listed.
Structural basis of coagulation factor V recognition for cleavage by RVV-V. Nakayama, D., Ben Ammar, Y., Miyata, T. et al. FEBS Lett (2011) 585:3020-3025. DOI 10.1016/j.febslet.2011.08.022 · PubMed
Other PDB entries of the same protein (UniProt P18965 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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