Crystal Structure of Double Mutant L380R/F535K of Human Acetylcholinesterase. Determined by X-ray diffraction at 2.08 Å resolution. Released 1 May 2019.
Explore 6O69 in 3D Show helices and sheets RCSB PDB PDBe
6O69 contains 37 α-helices and 28 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 | 6-8 | 3 | |
| β-strand | 9-12 | 4 | 1 |
| β-strand | 15-18 | 4 | 1 |
| β-strand | 20-22 | 3 | 2 |
| β-strand | 29-32 | 4 | 2 |
| β-strand | 33 | 1 | 3 |
| β-strand | 34-36 | 3 | 2 |
| β-strand | 38 | 1 | 4 |
| α-helix | 43-45 | 3 | |
| α-helix | 49-50 | 2 | |
| β-strand | 52 | 1 | 4 |
| α-helix | 53-55 | 3 | |
| β-strand | 59-61 | 3 | 1 |
| β-strand | 63 | 1 | 3 |
| α-helix | 67 | 1 | |
| β-strand | 68-69 | 2 | 5 |
| α-helix | 81-84 | 4 | |
| β-strand | 92-93 | 2 | 5 |
| β-strand | 98-104 | 7 | 2 |
| α-helix | 107-108 | 2 | |
| α-helix | 111 | 1 | |
| β-strand | 112-118 | 7 | 2 |
| α-helix | 131-133 | 3 | |
| α-helix | 136-142 | 7 | |
| β-strand | 145-149 | 5 | 2 |
| α-helix | 154-158 | 5 | |
| β-strand | 160 | 1 | 6 |
| β-strand | 168 | 1 | 6 |
| α-helix | 171-186 | 16 | |
| α-helix | 187-190 | 4 | |
| β-strand | 192-202 | 11 | 2 |
| α-helix | 204-213 | 10 | |
| α-helix | 216-219 | 4 | |
| β-strand | 224-228 | 5 | 2 |
| β-strand | 239 | 1 | 7 |
| α-helix | 241-255 | 15 | |
| α-helix | 266-273 | 8 | |
| α-helix | 278-283 | 6 | |
| α-helix | 285-288 | 4 | |
| β-strand | 302 | 1 | 7 |
| α-helix | 312-318 | 7 | |
| β-strand | 325-331 | 7 | 2 |
| β-strand | 333 | 1 | 8 |
| α-helix | 336-339 | 4 | |
| α-helix | 356-366 | 11 | |
| α-helix | 372-382 | 11 | |
| α-helix | 391-403 | 13 | |
| α-helix | 404-408 | 5 | |
| α-helix | 409-420 | 12 | |
| β-strand | 424-430 | 7 | 2 |
| α-helix | 432-434 | 3 | |
| α-helix | 441-443 | 3 | |
| β-strand | 446 | 1 | 8 |
| α-helix | 451-454 | 4 | |
| α-helix | 457-459 | 3 | |
| α-helix | 467-486 | 20 | |
| α-helix | 498 | 1 | |
| α-helix | 501-502 | 2 | |
| β-strand | 503 | 1 | 2 |
| β-strand | 509-513 | 5 | 2 |
| α-helix | 517-518 | 2 | |
| β-strand | 519-522 | 4 | 2 |
| α-helix | 526-530 | 5 | |
| α-helix | 531-535 | 5 | |
| α-helix | 536-539 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acetylcholinesterase | A | protein | 542 | Homo sapiens | P22303 (AlphaFold model) |
>6O69_1 Acetylcholinesterase (chains A) GREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVD ATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGG GFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQ WVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGM GEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVP VVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLA GVRVGVPQVSDLAAEAVVRHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQ GARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWA NFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRKLPKLLS AT
The structural and biochemical impacts of monomerizing human acetylcholinesterase. Bester, S.M., Adipietro, K.A., Funk, V.L. et al. Protein Sci (2019) 28:1106-1114. DOI 10.1002/pro.3625 · PubMed
Other PDB entries of the same protein (UniProt P22303 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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