Lysosomal glucocerebrosidase in complex with a stabilizing nanobody. Determined by X-ray diffraction at 1.7 Å resolution. Released 4 Jun 2025.
Explore 9ENA in 3D Show helices and sheets RCSB PDB PDBe
9ENA contains 25 α-helices and 40 β-strands across 2 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 | 2 | 1 | 1 |
| β-strand | 6-8 | 3 | 2 |
| β-strand | 14-18 | 5 | 2 |
| β-strand | 25 | 1 | 1 |
| α-helix | 27-29 | 3 | |
| α-helix | 31-33 | 3 | |
| β-strand | 36-43 | 8 | 3 |
| β-strand | 50-55 | 6 | 3 |
| α-helix | 56 | 1 | |
| β-strand | 57 | 1 | 3 |
| β-strand | 65-77 | 13 | 3 |
| α-helix | 78 | 1 | |
| β-strand | 80-84 | 5 | 4 |
| α-helix | 87-94 | 8 | |
| α-helix | 98-109 | 12 | |
| β-strand | 118-123 | 6 | 4 |
| α-helix | 151 | 1 | |
| α-helix | 152-157 | 6 | |
| α-helix | 158-167 | 10 | |
| β-strand | 173-178 | 6 | 4 |
| α-helix | 183-185 | 3 | |
| β-strand | 186 | 1 | 5 |
| β-strand | 197 | 1 | 5 |
| α-helix | 204-222 | 19 | |
| β-strand | 225 | 1 | 6 |
| β-strand | 229-231 | 3 | 4 |
| α-helix | 236-240 | 5 | |
| α-helix | 253-259 | 7 | |
| α-helix | 260-264 | 5 | |
| α-helix | 265-269 | 5 | |
| β-strand | 277-284 | 8 | 4 |
| α-helix | 285-287 | 3 | |
| α-helix | 290-296 | 7 | |
| α-helix | 299-302 | 4 | |
| β-strand | 307-313 | 7 | 4 |
| α-helix | 321-325 | 5 | |
| α-helix | 326-330 | 5 | |
| β-strand | 335-342 | 8 | 4 |
| α-helix | 357-372 | 16 | |
| β-strand | 377-382 | 6 | 4 |
| β-strand | 385 | 1 | 2 |
| β-strand | 402-405 | 4 | 2 |
| α-helix | 406-408 | 3 | |
| β-strand | 410-413 | 4 | 2 |
| α-helix | 415-424 | 10 | |
| β-strand | 432-438 | 7 | 3 |
| β-strand | 445-450 | 6 | 3 |
| β-strand | 456-462 | 7 | 3 |
| β-strand | 468-474 | 7 | 3 |
| β-strand | 478-484 | 7 | 3 |
| β-strand | 488-494 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 7 |
| β-strand | 12-14 | 3 | 8 |
| β-strand | 20-27 | 8 | 7 |
| β-strand | 35-41 | 7 | 8 |
| β-strand | 48-53 | 6 | 8 |
| β-strand | 60-62 | 3 | 8 |
| β-strand | 70-75 | 6 | 7 |
| β-strand | 80-85 | 6 | 7 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-101 | 8 | 8 |
| α-helix | 106-109 | 4 | |
| β-strand | 112 | 1 | 6 |
| β-strand | 119-122 | 4 | 8 |
| β-strand | 126-130 | 5 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucosylceramidase | A | protein | 497 | Homo sapiens | P04062 (AlphaFold model) |
| Chains: B | B | protein | 142 | Lama glama |
>9ENA_1 Glucosylceramidase (chains A) ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANH TGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIR VPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWT SPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGL LSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPE AAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRG MQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHL GHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFL ETISPGYSIHTYLWHRQ
>9ENA_2 Chains: B (chains B) MAQVQLVESGGGLVQPGGSLRLSCAASGFTLDYYAIGWFRQAPGKEREGVSCISSSDGST YYADSAKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCATDRGQCTYYSSGYYRDLRWYD YWGQGTQVTVSSHHHHHHEPEA
Water and common crystallization additives (SO4) are not listed.
Developing nanobodies as allosteric molecular chaperones of glucocerebrosidase function. Dal Maso, T., Sinisgalli, C., Zilio, G. et al. Nat Commun (2025) 16:4890-4890. DOI 10.1038/s41467-025-60134-4 · PubMed
Other PDB entries of the same protein (UniProt P04062 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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