Crystal structure of fviia in complex with a benzamidine-based inhibitor. Determined by X-ray diffraction at 1.57 Å resolution. Released 9 Oct 2024.
Explore 8QOD in 3D Show helices and sheets RCSB PDB PDBe
8QOD contains 36 α-helices and 50 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 4-8 | 5 | |
| α-helix | 10-11 | 2 | |
| α-helix | 13 | 1 | |
| α-helix | 14-19 | 6 | |
| α-helix | 24-31 | 8 | |
| α-helix | 34-46 | 13 | |
| α-helix | 49-52 | 4 | |
| β-strand | 60-64 | 5 | 1 |
| β-strand | 67-71 | 5 | 1 |
| β-strand | 76-77 | 2 | 2 |
| β-strand | 83-84 | 2 | 2 |
| α-helix | 85-87 | 3 | |
| α-helix | 94-97 | 4 | |
| β-strand | 101-103 | 3 | 3 |
| β-strand | 111-113 | 3 | 3 |
| β-strand | 118-120 | 3 | 4 |
| β-strand | 127-129 | 3 | 4 |
| α-helix | 139-141 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 5 |
| β-strand | 20-21 | 2 | 6 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 7 |
| β-strand | 39-46 | 8 | 7 |
| β-strand | 51-54 | 4 | 7 |
| α-helix | 56-59 | 4 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 7 |
| β-strand | 72 | 1 | 8 |
| β-strand | 81-91 | 11 | 7 |
| β-strand | 104-108 | 5 | 7 |
| α-helix | 111-114 | 4 | |
| β-strand | 115 | 1 | 9 |
| β-strand | 118 | 1 | 9 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 6 |
| α-helix | 123-125 | 3 | |
| α-helix | 126-129B | 6 | |
| α-helix | 129D-129F | 3 | |
| β-strand | 135-140 | 6 | 6 |
| β-strand | 143 | 1 | 10 |
| α-helix | 150 | 1 | |
| β-strand | 151 | 1 | 10 |
| α-helix | 152 | 1 | |
| β-strand | 154 | 1 | 8 |
| β-strand | 156-163 | 8 | 6 |
| α-helix | 165-170A | 7 | |
| α-helix | 170C-170D | 2 | |
| α-helix | 170H-175 | 3 | |
| β-strand | 180-183 | 4 | 6 |
| β-strand | 189 | 1 | 5 |
| β-strand | 198-203 | 6 | 6 |
| β-strand | 206-215 | 10 | 6 |
| β-strand | 226-230 | 5 | 6 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-242 | 8 | |
| α-helix | 245-246 | 2 | |
| β-strand | 251-254 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-17 | 8 | 11 |
| β-strand | 20-26 | 7 | 11 |
| β-strand | 32-40 | 9 | 12 |
| α-helix | 44-45 | 2 | |
| β-strand | 46-52 | 7 | 12 |
| β-strand | 56-58 | 3 | 11 |
| α-helix | 60-63 | 4 | |
| β-strand | 71-79 | 9 | 12 |
| α-helix | 91-92 | 2 | |
| β-strand | 93-96 | 4 | 12 |
| α-helix | 97-99 | 3 | |
| β-strand | 100 | 1 | 12 |
| α-helix | 102-105 | 4 | |
| β-strand | 107 | 1 | 11 |
| α-helix | 108-111 | 4 | |
| β-strand | 113-118 | 6 | 13 |
| β-strand | 122-127 | 6 | 13 |
| α-helix | 128-129 | 2 | |
| β-strand | 131-136 | 6 | 14 |
| β-strand | 139-142 | 4 | 14 |
| α-helix | 143-147 | 5 | |
| α-helix | 148-150 | 3 | |
| β-strand | 152-159 | 8 | 15 |
| β-strand | 166-170 | 5 | 15 |
| β-strand | 174-178 | 5 | 13 |
| β-strand | 185-192 | 8 | 15 |
| β-strand | 201 | 1 | 15 |
| α-helix | 203-207 | 5 | |
| β-strand | 208-209 | 2 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Factor VII light chain | A | protein | 141 | Homo sapiens | P08709 (AlphaFold model) |
| Coagulation factor VII | B | protein | 254 | Homo sapiens | P08709 (AlphaFold model) |
| Tissue factor | C | protein | 243 | Homo sapiens | P13726 (AlphaFold model) |
>8QOD_1 Factor VII light chain (chains A) AFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCK DQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLA DGVSCTPTVEYPCGKIPILEK
>8QOD_2 Coagulation factor VII (chains B) IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHD LSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERT LAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGY SDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMR SEPRPGVLLRAPFP
>8QOD_3 Tissue factor (chains C) METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPK PVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGS AGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFG KDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVE CMG
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 4 |
| MG | Magnesium ion | Mg | 1 |
| WIZ | 3-[2-bromanyl-4-[(1~{S})-1-[[3-[(4-carbamimidoylphenyl)amino]-3-oxidanylidene-p… | C25 H23 Br N4 O5 | 1 |
| FUC | alpha-L-fucopyranose | C6 H12 O5 | 1 |
| GLC | alpha-D-glucopyranose | C6 H12 O6 | 1 |
Water and common crystallization additives (CL) are not listed.
Crystallography and molecular simulations capture S1 pocket collapse in allosteric regulation of factor VIIa and other serine proteases. Tesmer, L., Hans Matter, H., Klingler, O. et al. To be published.
Other PDB entries of the same protein (UniProt P08709 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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