Energetic and structural effects of the Tanford transition on the ligand recognition of bovine Beta-lactoglobulin. Determined by X-ray diffraction at 1.74 Å resolution. Released 27 Jan 2021.
Explore 7KOT in 3D Show helices and sheets RCSB PDB PDBe
7KOT 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 |
|---|---|---|---|
| α-helix | 12-15 | 4 | |
| β-strand | 17-18 | 2 | 1 |
| β-strand | 20-26 | 7 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 41-48 | 8 | 1 |
| β-strand | 54-62 | 9 | 1 |
| β-strand | 65-75 | 11 | 1 |
| β-strand | 81-84 | 4 | 1 |
| β-strand | 91-97 | 7 | 1 |
| β-strand | 102-108 | 7 | 1 |
| β-strand | 117-123 | 7 | 1 |
| α-helix | 130-140 | 11 | |
| β-strand | 147-150 | 4 | 1 |
| α-helix | 153-156 | 4 | |
| α-helix | 159-161 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-lactoglobulin | A | protein | 162 | Bos taurus | P02754 (AlphaFold model) |
>7KOT_1 Beta-lactoglobulin (chains A) LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQK WENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQ CLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
| ID | Name | Formula | Copies |
|---|---|---|---|
| SDS | Dodecyl sulfate | C12 H26 O4 S | 1 |
Energetic and structural effects of the Tanford transition on ligand recognition of bovine beta-lactoglobulin. Labra-Nunez, A., Cofas-Vargas, L.F., Gutierrez-Magdaleno, G. et al. Arch Biochem Biophys (2021) 699:108750-108750. DOI 10.1016/j.abb.2020.108750 · PubMed
Other PDB entries of the same protein (UniProt P02754 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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