Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA). Determined by X-ray diffraction at 2.05 Å resolution. Released 21 Sept 2004.
Explore 1O5D in 3D Show helices and sheets RCSB PDB PDBe
1O5D contains 17 α-helices and 47 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 |
|---|---|---|---|
| β-strand | 17 | 1 | 5 |
| β-strand | 20-21 | 2 | 6 |
| β-strand | 30-35 | 6 | 7 |
| β-strand | 39-48 | 10 | 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 |
| β-strand | 115 | 1 | 9 |
| β-strand | 118 | 1 | 9 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 6 |
| 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 | |
| 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 | 231-233 | 3 | |
| α-helix | 235-241 | 7 | |
| β-strand | 251-254 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 50-52 | 3 | |
| β-strand | 60-63 | 4 | 1 |
| β-strand | 68-71 | 4 | 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 | 101-105 | 5 | 3 |
| β-strand | 108-113 | 6 | 3 |
| β-strand | 118-120 | 3 | 4 |
| β-strand | 127-129 | 3 | 4 |
| α-helix | 139-141 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-17 | 8 | 11 |
| β-strand | 20-26 | 7 | 11 |
| β-strand | 32-40 | 9 | 12 |
| β-strand | 46-52 | 7 | 12 |
| β-strand | 56-58 | 3 | 11 |
| α-helix | 60-63 | 4 | |
| β-strand | 71-79 | 9 | 12 |
| β-strand | 87 | 1 | 13 |
| β-strand | 91 | 1 | 13 |
| β-strand | 93-96 | 4 | 12 |
| β-strand | 100 | 1 | 12 |
| α-helix | 102-105 | 4 | |
| β-strand | 107 | 1 | 11 |
| β-strand | 131-136 | 6 | 14 |
| β-strand | 139-142 | 4 | 14 |
| α-helix | 143-147 | 5 | |
| β-strand | 152-154 | 3 | 15 |
| β-strand | 190-192 | 3 | 15 |
| β-strand | 201 | 1 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Coagulation factor VII | L | protein | 152 | Homo sapiens | P08709 (AlphaFold model) |
| Coagulation factor VII | H | protein | 254 | Homo sapiens | P08709 (AlphaFold model) |
| Tissue factor | T | protein | 218 | Homo sapiens | P13726 (AlphaFold model) |
>1O5D_1 Coagulation factor VII (chains L) ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGS CKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILEKRNASKPQGR
>1O5D_2 Coagulation factor VII (chains H) IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHD LSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERT LAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGY SDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMR SEPRPGVLLRAPFP
>1O5D_3 Tissue factor (chains T) GTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTD EIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGT KVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDK GENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFRE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CR9 | 2-{5-[amino(iminio)methyl]-6-fluoro-1H-benzimidazol-2-yl}-6-[(2-methylcyclohexy… | C21 H23 F N4 O2 | 1 |
Dissecting and designing inhibitor selectivity determinants at the S1 site using an artificial Ala190 protease (Ala190 uPA). Katz, B.A., Luong, C., Ho, J.D. et al. J Mol Biol (2004) 344:527-547. DOI 10.1016/j.jmb.2004.09.032 · PubMed
Other PDB entries of the same protein (UniProt P08709 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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