Complex of active site inhibited human blood coagulation factor VIIA with human recombinant soluble tissue factor. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Sept 1997.
Explore 1DAN in 3D Show helices and sheets RCSB PDB PDBe
1DAN contains 32 α-helices and 50 β-strands across 4 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 |
| 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 | |
| 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 | 165-170 | 6 | |
| 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 | |
| β-strand | 251-254 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 10-11 | 2 | |
| α-helix | 13 | 1 | |
| α-helix | 14-18 | 5 | |
| 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 |
| α-helix | 72-73 | 2 | |
| β-strand | 76-77 | 2 | 2 |
| β-strand | 83-84 | 2 | 2 |
| α-helix | 85-88 | 4 | |
| 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 | 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| 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 | 113-119 | 7 | 13 |
| β-strand | 122-127 | 6 | 13 |
| β-strand | 131-136 | 6 | 14 |
| β-strand | 139-142 | 4 | 14 |
| α-helix | 143-147 | 5 | |
| α-helix | 148-150 | 3 | |
| β-strand | 152-157 | 6 | 15 |
| β-strand | 166-170 | 5 | 15 |
| β-strand | 174-178 | 5 | 13 |
| β-strand | 186-192 | 7 | 15 |
| β-strand | 201 | 1 | 15 |
| α-helix | 203-207 | 5 | |
| β-strand | 208-209 | 2 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| BLOOD COAGULATION FACTOR VIIA light chain | L | protein | 152 | Homo sapiens | P08709 (AlphaFold model) |
| BLOOD COAGULATION FACTOR VIIA heavy chain | H | protein | 254 | Homo sapiens | P08709 (AlphaFold model) |
| Soluble tissue factor | T | protein | 80 | Homo sapiens | P13726 (AlphaFold model) |
| Soluble tissue factor | U | protein | 121 | Homo sapiens | P13726 (AlphaFold model) |
>1DAN_1 BLOOD COAGULATION FACTOR VIIA light chain (chains L) ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGS CKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILEKRNASKPQGR
>1DAN_2 BLOOD COAGULATION FACTOR VIIA heavy chain (chains H) IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHD LSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERT LAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGY SDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMR SEPRPGVLLRAPFP
>1DAN_3 SOLUBLE TISSUE FACTOR (chains T) NTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIV KDVKQTYLARVFSYPAGNVE
>1DAN_4 SOLUBLE TISSUE FACTOR (chains U) GEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGK DLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVEC M
| ID | Name | Formula | Copies |
|---|---|---|---|
| 0Z6 | D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexa… | C25 H36 Cl N6 O3 | 1 |
| CAC | Cacodylate ion | C2 H6 As O2 | 1 |
| CA | Calcium ion | Ca | 9 |
| FUC | alpha-L-fucopyranose | C6 H12 O5 | 1 |
| BGC | beta-D-glucopyranose | C6 H12 O6 | 1 |
Water and common crystallization additives (CL) are not listed.
The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Banner, D.W., D'Arcy, A., Chene, C. et al. Nature (1996) 380:41-46. DOI 10.1038/380041a0 · PubMed
Other PDB entries of the same protein (UniProt P08709 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1DAN is part of these collections:
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