Structure of recombinant human beta-glucocerebrosidase in complex with L-carbaxylosyl chloride. Determined by X-ray diffraction at 1.49 Å resolution. Released 13 Mar 2024.
Explore 8AWR in 3D Show helices and sheets RCSB PDB PDBe
8AWR contains 25 α-helices and 27 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 |
|---|---|---|---|
| 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 | |
| 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 | |
| α-helix | 171-172 | 2 | |
| 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 | 229-231 | 3 | 4 |
| α-helix | 238-240 | 3 | |
| 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 | 307-311 | 5 | 4 |
| α-helix | 315-317 | 3 | |
| α-helix | 320 | 1 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-330 | 5 | |
| β-strand | 335-340 | 6 | 4 |
| α-helix | 357-372 | 16 | |
| β-strand | 375-382 | 8 | 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 | 444-450 | 7 | 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysosomal acid glucosylceramidase | AAA | protein | 497 | Homo sapiens | P04062 (AlphaFold model) |
>8AWR_1 Lysosomal acid glucosylceramidase (chains AAA) ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANH TGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIR VPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWT SPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGL LSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPE AAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRG MQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHL GHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFL ETISPGYSIHTYLWRRQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
| OIZ | (1~{S},2~{R},3~{S},6~{S})-6-chloranylcyclohex-4-ene-1,2,3-triol | C6 H9 Cl O3 | 1 |
| OJ6 | (1~{S},2~{S},3~{S},4~{R})-cyclohexane-1,2,3,4-tetrol | C6 H12 O4 | 1 |
Water and common crystallization additives (SO4, EDO, PEG, NA) are not listed.
Single turnover covalent inhibitors for functional chaperoning of lysosomal glycoside hydrolases. Bhosale, S., Kandalkar, S., Gilormini, P.A. et al. To be published.
Other PDB entries of the same protein (UniProt P04062 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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