The solution structure of the second kunitz domain of tissue factor pathway inhibitor, NMR, 30 structures. Determined by solution NMR. Released 25 Feb 1998.
Explore 1ADZ in 3D Show helices and sheets RCSB PDB PDBe
1ADZ contains 5 α-helices and 3 β-strands across 1 chain. 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 | 12-15 | 4 | |
| α-helix | 17-18 | 2 | |
| β-strand | 29-33 | 5 | 1 |
| α-helix | 34-36 | 3 | |
| β-strand | 38-42 | 5 | 1 |
| β-strand | 54 | 1 | 1 |
| α-helix | 57-60 | 4 | |
| α-helix | 61-65 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tissue factor pathway inhibitor | A | protein | 71 | Homo sapiens | P10646 (AlphaFold model) |
>1ADZ_1 TISSUE FACTOR PATHWAY INHIBITOR (chains A) DYKDDDDKLKPDFCFLEEDPGICRGYITRYFYNNQTKQCERFKYGGCLGNMNNFETLEEC KNICEDGPNGF
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 P10646 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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