Structure of apo form of human gamma-secretase PSEN1 APH-1B isoform reconstituted into lipid nanodisc. Determined by electron microscopy at 3.3 Å resolution. Released 24 Apr 2024.
Explore 8OQY in 3D Show helices and sheets RCSB PDB PDBe
8OQY contains 57 α-helices and 33 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 | 35-39 | 5 | |
| β-strand | 42-43 | 2 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 50-51 | 2 | |
| β-strand | 53-54 | 2 | 2 |
| β-strand | 59-60 | 2 | 2 |
| β-strand | 61-62 | 2 | 3 |
| β-strand | 69-73 | 5 | 1 |
| α-helix | 79-86 | 8 | |
| β-strand | 94-99 | 6 | 1 |
| α-helix | 105-113 | 9 | |
| β-strand | 120-124 | 5 | 1 |
| α-helix | 125-126 | 2 | |
| β-strand | 135 | 1 | 4 |
| α-helix | 154-156 | 3 | |
| β-strand | 168 | 1 | 4 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-176 | 2 | 3 |
| β-strand | 180-183 | 4 | 1 |
| α-helix | 186-199 | 14 | |
| α-helix | 207-209 | 3 | |
| β-strand | 212-217 | 6 | 1 |
| α-helix | 227-239 | 13 | |
| β-strand | 248-250 | 3 | 2 |
| β-strand | 253-259 | 7 | 5 |
| β-strand | 275-281 | 7 | 5 |
| α-helix | 295-299 | 5 | |
| α-helix | 300-313 | 14 | |
| α-helix | 318-320 | 3 | |
| β-strand | 324-330 | 7 | 5 |
| α-helix | 338-348 | 11 | |
| α-helix | 356-358 | 3 | |
| β-strand | 359-365 | 7 | 5 |
| β-strand | 375-379 | 5 | 5 |
| α-helix | 384-386 | 3 | |
| α-helix | 388-406 | 19 | |
| β-strand | 412-414 | 3 | 5 |
| α-helix | 421-423 | 3 | |
| α-helix | 427-431 | 5 | |
| β-strand | 438-442 | 5 | 5 |
| α-helix | 460-463 | 4 | |
| α-helix | 473-477 | 5 | |
| α-helix | 482-501 | 20 | |
| α-helix | 515-526 | 12 | |
| α-helix | 532-535 | 4 | |
| β-strand | 539 | 1 | 6 |
| α-helix | 540-545 | 6 | |
| α-helix | 562-575 | 14 | |
| β-strand | 577-579 | 3 | 6 |
| α-helix | 583-587 | 5 | |
| α-helix | 589-591 | 3 | |
| β-strand | 601-605 | 5 | 6 |
| β-strand | 609 | 1 | 7 |
| β-strand | 616 | 1 | 7 |
| β-strand | 619-623 | 5 | 6 |
| β-strand | 626-630 | 5 | 5 |
| α-helix | 633-636 | 4 | |
| β-strand | 649-651 | 3 | 2 |
| β-strand | 658-663 | 6 | 1 |
| α-helix | 666-692 | 27 | |
| α-helix | 694-697 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 74-103 | 30 | |
| α-helix | 162-189 | 28 | |
| β-strand | 193-194 | 2 | 8 |
| α-helix | 195-213 | 19 | |
| α-helix | 219-240 | 22 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-255 | 10 | |
| α-helix | 384-397 | 14 | |
| α-helix | 405-427 | 23 | |
| α-helix | 437-448 | 12 | |
| α-helix | 449-453 | 5 | |
| α-helix | 454-462 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-24 | 22 | |
| α-helix | 25-27 | 3 | |
| α-helix | 29-60 | 32 | |
| α-helix | 65-99 | 35 | |
| α-helix | 113-137 | 25 | |
| α-helix | 138-140 | 3 | |
| β-strand | 145 | 1 | 1 |
| α-helix | 155-182 | 28 | |
| α-helix | 186-205 | 20 | |
| α-helix | 209-230 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-21 | 14 | |
| α-helix | 27-41 | 15 | |
| α-helix | 50-81 | 32 | |
| α-helix | 83-85 | 3 | |
| α-helix | 87-92 | 6 | |
| β-strand | 93-94 | 2 | 8 |
| α-helix | 96-97 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nicastrin | A | protein | 717 | Homo sapiens | Q92542 (AlphaFold model) |
| Presenilin-1 CTF12 | B | protein | 467 | Homo sapiens | P49768 (AlphaFold model) |
| Gamma-secretase subunit APH-1B | C | protein | 257 | Homo sapiens | Q8WW43 (AlphaFold model) |
| Gamma-secretase subunit PEN-2 | D | protein | 101 | Homo sapiens | Q9NZ42 (AlphaFold model) |
>8OQY_1 Nicastrin (chains A) MATAGGGSGADPGSRGLLRLLSFCVLLAGLCRGNSVERKIYIPLNKTAPCVRLLNATHQI GCQSSISGDTGVIHVVEKEEDLQWVLTDGPNPPYMVLLESKHFTRDLMEKLKGRTSRIAG LAVSLTKPSPASGFSPSVQCPNDGFGVYSNSYGPEFAHCREIQWNSLGNGLAYEDFSFPI FLLEDENETKVIKQCYQDHNLSQNGSAPTFPLCAMQLFSHMHAVISTATCMRRSSIQSTF SINPEIVCDPLSDYNVWSMLKPINTTGTLKPDDRVVVAATRLDSRSFFWNVAPGAESAVA SFVTQLAAAEALQKAPDVTTLPRNVMFVFFQGETFDYIGSSRMVYDMEKGKFPVQLENVD SFVELGQVALRTSLELWMHTDPVSQKNESVRNQVEDLLATLEKSGAGVPAVILRRPNQSQ PLPPSSLQRFLRARNISGVVLADHSGAFHNKYYQSIYDTAENINVSYPEWLSPEEDLNFV TDTAKALADVATVLGRALYELAGGTNFSDTVQADPQTVTRLLYGFLIKANNSWFQSILRQ DLRSYLGDGPLQHYIAVSSPTNTTYVVQYALANLTGTVVNLTREQCQDPSKVPSENKDLY EYSWVQGPLHSNETDRLPRCVRSTARLARALSPAFELSQWSSTEYSTWTESRWKDIRARI FLIASKELELITLTVGFGILIFSLIVTYCINAKADVLFIAPREPGAVSYGTLEVLFQ
>8OQY_2 Presenilin-1 CTF12 (chains B) MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSR QVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTE DTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFI YLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKY LPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAE GDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAA VQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCL TLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI
>8OQY_3 Gamma-secretase subunit APH-1B (chains C) MTAAVFFGCAFIAFGPALALYVFTIATEPLRIIFLIAGAFFWLVSLLISSLVWFMARVII DNKDGPTQKYLLIFGAFVSVYIQEMFRFAYYKLLKKASEGLKSINPGETAPSMRLLAYVS GLGFGIMSGVFSFVNTLSDSLGPGTVGIHGDSPQFFLYSAFMTLVIILLHVFWGIVFFDG CEKKKWGILLIVLLTHLLVSAQTFISSYYGINLASAFIILVLMGTWAFLAAGGSCRSLKL CLLCQDKNFLLYNQRSR
>8OQY_4 Gamma-secretase subunit PEN-2 (chains D) MNLERVSNEEKLNLCRKYYLGGFAFLPFLWLVNIFWFFREAFLVPAYTEQSQIKGYVWRS AVGFLFWVIVLTSWITIFQIYRPRWGALGDYLSFTIPLGTP
| ID | Name | Formula | Copies |
|---|---|---|---|
| PC1 | 1,2-diacyl-sn-glycero-3-phosphocholine | C44 H88 N O8 P | 3 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 7 |
Apo and A beta 46-bound gamma-secretase structures provide insights into amyloid-beta processing by the APH-1B isoform. Odorcic, I., Hamed, M.B., Lismont, S. et al. Nat Commun (2024) 15:4479-4479. DOI 10.1038/s41467-024-48776-2 · PubMed
Other PDB entries of the same protein (UniProt Q92542 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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