Orally available Factor7a inhibitor. Determined by X-ray diffraction at 1.6 Å resolution. Released 22 Feb 2006.
Explore 2BZ6 in 3D Show helices and sheets RCSB PDB PDBe
2BZ6 contains 15 α-helices and 27 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 |
| β-strand | 30-35 | 6 | 3 |
| β-strand | 39-46 | 8 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-59 | 4 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-91 | 11 | 3 |
| β-strand | 104-108 | 5 | 3 |
| α-helix | 111-114 | 4 | |
| β-strand | 115 | 1 | 5 |
| β-strand | 118 | 1 | 5 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 126-129B | 6 | |
| α-helix | 129D-129F | 3 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 143 | 1 | 6 |
| α-helix | 150 | 1 | |
| β-strand | 151 | 1 | 6 |
| α-helix | 152 | 1 | |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 165-170A | 7 | |
| α-helix | 170C-170D | 2 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| α-helix | 192-194 | 3 | |
| β-strand | 198-203 | 6 | 2 |
| β-strand | 206-215 | 10 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-242 | 8 | |
| α-helix | 245-246 | 2 | |
| β-strand | 251-254 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 94-97 | 4 | |
| β-strand | 101-105 | 5 | 7 |
| β-strand | 109-113 | 5 | 7 |
| β-strand | 118-120 | 3 | 8 |
| β-strand | 127-129 | 3 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Blood coagulation factor viia | H | protein | 254 | HOMO SAPIENS | P08709 (AlphaFold model) |
| Blood coagulation factor viia | L | protein | 53 | HOMO SAPIENS | P08709 (AlphaFold model) |
>2BZ6_1 BLOOD COAGULATION FACTOR VIIA (chains H) IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHD LSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERT LAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGY SDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMR SEPRPGVLLRAPFP
>2BZ6_2 BLOOD COAGULATION FACTOR VIIA (chains L) ICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
| 346 | (r)-(4-carbamimidoyl-phenylamino)-[5-ethoxy-2-fluoro-3-[(R)-tetrahydro-furan-3-… | C21 H24 F N3 O5 | 1 |
Water and common crystallization additives (SO4) are not listed.
Dose-Dependant Antithrombotic Activity of an Orally Active Tissue Factor/Factor Viia Inhibitor without Concomitant Enhancement of Bleeding Propensity. Groebke-Zbinden, K., Banner, D.W., Hilpert, K. et al. Bioorg Med Chem (2006) 14:5357. DOI 10.1016/J.BMC.2006.03.042 · 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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