Crystal structure of Lecithin:cholesterol acyltransferase (LCAT) in a closed conformation. Determined by X-ray diffraction at 3.1 Å resolution. Released 25 Oct 2017.
Explore 5TXF in 3D Show helices and sheets RCSB PDB PDBe
5TXF contains 76 α-helices and 96 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 |
|---|---|---|---|
| α-helix | 21-24 | 4 | |
| β-strand | 25-28 | 4 | 1 |
| β-strand | 36-40 | 5 | 2 |
| β-strand | 41 | 1 | 3 |
| β-strand | 53 | 1 | 3 |
| β-strand | 58-61 | 4 | 2 |
| α-helix | 64-67 | 4 | |
| α-helix | 71-79 | 9 | |
| β-strand | 81-84 | 4 | 4 |
| β-strand | 89-92 | 4 | 4 |
| β-strand | 96-99 | 4 | 2 |
| α-helix | 107-110 | 4 | |
| β-strand | 111 | 1 | 5 |
| β-strand | 119 | 1 | 5 |
| α-helix | 122-130 | 9 | |
| β-strand | 135 | 1 | 1 |
| β-strand | 139-141 | 3 | 1 |
| α-helix | 150-152 | 3 | |
| α-helix | 154-171 | 18 | |
| α-helix | 174 | 1 | |
| β-strand | 175-180 | 6 | 1 |
| α-helix | 182-193 | 12 | |
| α-helix | 196-202 | 7 | |
| β-strand | 203-209 | 7 | 1 |
| α-helix | 218-224 | 7 | |
| β-strand | 234 | 1 | 5 |
| α-helix | 250-252 | 3 | |
| β-strand | 264-267 | 4 | 6 |
| β-strand | 272-274 | 3 | 6 |
| α-helix | 275-277 | 3 | |
| α-helix | 278-284 | 7 | |
| α-helix | 288-297 | 10 | |
| β-strand | 311-317 | 7 | 1 |
| β-strand | 319-326 | 8 | 6 |
| α-helix | 335-336 | 2 | |
| β-strand | 338-345 | 8 | 6 |
| β-strand | 349 | 1 | 6 |
| α-helix | 350-353 | 4 | |
| α-helix | 355-359 | 5 | |
| β-strand | 360 | 1 | 7 |
| β-strand | 363 | 1 | 7 |
| β-strand | 367-373 | 7 | 1 |
| α-helix | 384-394 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphatidylcholine-sterol acyltransferase | A, B, C, D | protein | 422 | Homo sapiens | P04180 (AlphaFold model) |
>5TXF_1 Phosphatidylcholine-sterol acyltransferase (chains A, B, C, D) FWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTI WLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGY LHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGH SLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLK EEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDL LAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQ GRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPEHHHH HH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I. Manthei, K.A., Ahn, J., Glukhova, A. et al. J Biol Chem (2017) 292:20313-20327. DOI 10.1074/jbc.M117.802736 · PubMed
Other PDB entries of the same protein (UniProt P04180 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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