Complex of the second kunitz domain of tissue factor pathway inhibitor with porcine trypsin. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Jan 1998.
Explore 1TFX in 3D Show helices and sheets RCSB PDB PDBe
1TFX contains 26 α-helices and 46 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 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 3 |
| β-strand | 40-48 | 9 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-67 | 4 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-124 | 2 | |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-201 | 4 | 2 |
| β-strand | 204-215 | 8 | 2 |
| α-helix | 225 | 1 | |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-242 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 5 |
| β-strand | 20-21 | 2 | 6 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 7 |
| β-strand | 40-48 | 9 | 7 |
| β-strand | 51-54 | 4 | 7 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-67 | 4 | 7 |
| β-strand | 72 | 1 | 8 |
| β-strand | 81-90 | 10 | 7 |
| β-strand | 104-108 | 5 | 7 |
| α-helix | 111-113 | 3 | |
| β-strand | 122 | 1 | 6 |
| α-helix | 123-124 | 2 | |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 6 |
| β-strand | 154 | 1 | 8 |
| β-strand | 156-162 | 7 | 6 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 6 |
| β-strand | 189 | 1 | 5 |
| β-strand | 198-201 | 4 | 6 |
| β-strand | 204-215 | 8 | 6 |
| β-strand | 221B | 1 | 9 |
| β-strand | 224 | 1 | 9 |
| β-strand | 226-230 | 5 | 6 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| α-helix | 8-9 | 2 | |
| β-strand | 14 | 1 | 2 |
| β-strand | 18-24 | 7 | 10 |
| β-strand | 29-35 | 7 | 10 |
| β-strand | 45 | 1 | 10 |
| α-helix | 48-51 | 4 | |
| α-helix | 52-57 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| α-helix | 8-9 | 2 | |
| β-strand | 14 | 1 | 6 |
| β-strand | 18-24 | 7 | 11 |
| β-strand | 29-35 | 7 | 11 |
| β-strand | 45 | 1 | 11 |
| α-helix | 48-51 | 4 | |
| α-helix | 52-56 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trypsin | A, B | protein | 223 | Sus scrofa | P00761 (AlphaFold model) |
| Tissue factor pathway inhibitor | C, D | protein | 58 | Homo sapiens | P10646 (AlphaFold model) |
>1TFX_1 TRYPSIN (chains A, B) IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEG NEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISG WGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGP VVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
>1TFX_2 TISSUE FACTOR PATHWAY INHIBITOR (chains C, D) KPDFCFLEEDPGICRGYITRYFYNNQTKQCERFKYGGCLGNMNNFETLEECKNICEDG
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa. Burgering, M.J., Orbons, L.P., van der Doelen, A. et al. J Mol Biol (1997) 269:395-407. DOI 10.1006/jmbi.1997.1029 · PubMed
Other PDB entries of the same protein (UniProt P00761 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1TFX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.