The C-type lectin carbohydrate recognition domain of human tetranectin. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 May 1998.
Explore 1TN3 in 3D Show helices and sheets RCSB PDB PDBe
1TN3 contains 5 α-helices and 10 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 | 49-52 | 4 | 1 |
| β-strand | 58-68 | 11 | 1 |
| α-helix | 70-79 | 10 | |
| β-strand | 83-84 | 2 | 1 |
| α-helix | 90-103 | 14 | |
| β-strand | 109-119 | 11 | 2 |
| β-strand | 122-125 | 4 | 2 |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 2 |
| α-helix | 131 | 1 | |
| β-strand | 136 | 1 | 2 |
| α-helix | 147-149 | 3 | |
| β-strand | 152-156 | 5 | 2 |
| β-strand | 162-166 | 5 | 2 |
| β-strand | 172-179 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tetranectin | A | protein | 137 | Homo sapiens | P05452 (AlphaFold model) |
>1TN3_1 TETRANECTIN (chains A) ALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLSTPQTGSENDALYEYLRQSV GNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWF DKRCRDQLPYICQFGIV
Water and common crystallization additives (SO4) are not listed.
Structure of the C-type lectin carbohydrate recognition domain of human tetranectin. Kastrup, J.S., Nielsen, B.B., Rasmussen, H. et al. Acta Crystallogr D Biol Crystallogr (1998) 54:757-766. DOI 10.1107/S0907444997016806 · PubMed
Other PDB entries of the same protein (UniProt P05452 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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