Low resolution crystal structure of Lecithin:Cholesterol Acyltransferase (LCAT; residues 21-397). Determined by X-ray diffraction at 8.69 Å resolution. Released 25 Mar 2015.
Explore 4X96 in 3D Show helices and sheets RCSB PDB PDBe
4X96 contains 76 α-helices and 92 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 |
|---|---|---|---|
| β-strand | 25-28 | 4 | 8 |
| β-strand | 36-40 | 5 | 9 |
| β-strand | 41 | 1 | 10 |
| β-strand | 53 | 1 | 10 |
| β-strand | 58-61 | 4 | 9 |
| α-helix | 65-67 | 3 | |
| α-helix | 69-79 | 11 | |
| β-strand | 82 | 1 | 11 |
| β-strand | 91 | 1 | 11 |
| α-helix | 92-93 | 2 | |
| β-strand | 96-99 | 4 | 9 |
| α-helix | 107-110 | 4 | |
| β-strand | 111 | 1 | 12 |
| β-strand | 119 | 1 | 12 |
| α-helix | 122-131 | 10 | |
| β-strand | 135 | 1 | 8 |
| β-strand | 139-141 | 3 | 8 |
| α-helix | 150-152 | 3 | |
| α-helix | 154-171 | 18 | |
| β-strand | 175-180 | 6 | 8 |
| α-helix | 183-193 | 11 | |
| α-helix | 196-202 | 7 | |
| β-strand | 203-209 | 7 | 8 |
| α-helix | 219-224 | 6 | |
| α-helix | 236-243 | 8 | |
| α-helix | 248-251 | 4 | |
| β-strand | 264-267 | 4 | 13 |
| β-strand | 272-274 | 3 | 13 |
| α-helix | 275-277 | 3 | |
| α-helix | 278-284 | 7 | |
| α-helix | 288-298 | 11 | |
| β-strand | 311-313 | 3 | 8 |
| β-strand | 316-317 | 2 | 14 |
| β-strand | 319-326 | 8 | 13 |
| β-strand | 338-345 | 8 | 13 |
| β-strand | 349 | 1 | 13 |
| α-helix | 350-353 | 4 | |
| α-helix | 355-358 | 4 | |
| β-strand | 367-369 | 3 | 8 |
| β-strand | 372-373 | 2 | 14 |
| α-helix | 379-382 | 4 | |
| α-helix | 384-395 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphatidylcholine-sterol acyltransferase | A, B, C, D | protein | 383 | Homo sapiens | P04180 (AlphaFold model) |
>4X96_1 Phosphatidylcholine-sterol acyltransferase (chains A, B, C, D) HTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTR VVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVR AAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKD RFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWP EDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLP TPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNM VFSNLTLEHINAILLGAHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase. Glukhova, A., Hinkovska-Galcheva, V., Kelly, R. et al. Nat Commun (2015) 6:6250-6250. DOI 10.1038/ncomms7250 · 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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