The structure of a 19 residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin. Determined by solution NMR. Released 8 Jun 1995.
Explore 1TMR in 3D Show helices and sheets RCSB PDB PDBe
1TMR contains 0 α-helices and 2 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 |
|---|---|---|---|
| β-strand | 9 | 1 | 1 |
| β-strand | 12 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Thrombomodulin precursor | A | protein | 19 | Homo sapiens | P07204 (AlphaFold model) |
>1TMR_1 THROMBOMODULIN PRECURSOR (chains A) VCAEGFAPIPGEPHRCQLF
The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin. Adler, M., Seto, M.H., Nitecki, D.E. et al. J Biol Chem (1995) 270:23366-23372. DOI 10.1074/jbc.270.40.23366 · PubMed
Other PDB entries of the same protein (UniProt P07204 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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