Crystal Structure of Recombinant GBA in Complex with Bis-Tris Propane. Determined by X-ray diffraction at 1.56 Å resolution. Released 10 Jun 2020.
Explore 6TJK in 3D Show helices and sheets RCSB PDB PDBe
6TJK contains 53 α-helices and 52 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 |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| β-strand | 6-7 | 2 | 1 |
| α-helix | 14 | 1 | |
| β-strand | 15-18 | 4 | 1 |
| α-helix | 26-29 | 4 | |
| α-helix | 32-33 | 2 | |
| β-strand | 36-43 | 8 | 2 |
| β-strand | 50-55 | 6 | 2 |
| α-helix | 56 | 1 | |
| β-strand | 57 | 1 | 2 |
| β-strand | 65-77 | 13 | 2 |
| α-helix | 78 | 1 | |
| β-strand | 80-84 | 5 | 3 |
| α-helix | 87-95 | 9 | |
| α-helix | 98-109 | 12 | |
| β-strand | 118-123 | 6 | 3 |
| α-helix | 151 | 1 | |
| α-helix | 152-157 | 6 | |
| α-helix | 158-167 | 10 | |
| α-helix | 171-172 | 2 | |
| β-strand | 173-178 | 6 | 3 |
| α-helix | 183-185 | 3 | |
| β-strand | 186 | 1 | 4 |
| β-strand | 197 | 1 | 4 |
| α-helix | 204-222 | 19 | |
| β-strand | 229-231 | 3 | 3 |
| 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 | 3 |
| α-helix | 285-287 | 3 | |
| α-helix | 290-296 | 7 | |
| α-helix | 299-302 | 4 | |
| β-strand | 307-311 | 5 | 3 |
| α-helix | 315-317 | 3 | |
| α-helix | 320 | 1 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-330 | 5 | |
| β-strand | 335-340 | 6 | 3 |
| α-helix | 357-372 | 16 | |
| β-strand | 375-382 | 8 | 3 |
| β-strand | 385 | 1 | 1 |
| β-strand | 402-405 | 4 | 1 |
| α-helix | 406-408 | 3 | |
| β-strand | 410-413 | 4 | 1 |
| α-helix | 415-424 | 10 | |
| β-strand | 432-438 | 7 | 2 |
| β-strand | 444-450 | 7 | 2 |
| β-strand | 456-462 | 7 | 2 |
| β-strand | 468-474 | 7 | 2 |
| β-strand | 478-484 | 7 | 2 |
| β-strand | 488-494 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 5 |
| β-strand | 6-8 | 3 | 6 |
| β-strand | 14-18 | 5 | 6 |
| β-strand | 25 | 1 | 5 |
| α-helix | 26-29 | 4 | |
| α-helix | 31-33 | 3 | |
| β-strand | 36-43 | 8 | 7 |
| β-strand | 50-55 | 6 | 7 |
| β-strand | 57 | 1 | 7 |
| β-strand | 66-77 | 12 | 7 |
| α-helix | 78 | 1 | |
| β-strand | 80-84 | 5 | 8 |
| α-helix | 87-94 | 8 | |
| α-helix | 98-109 | 12 | |
| β-strand | 118-123 | 6 | 8 |
| α-helix | 151 | 1 | |
| α-helix | 152-157 | 6 | |
| α-helix | 158-167 | 10 | |
| α-helix | 171-172 | 2 | |
| β-strand | 173-178 | 6 | 8 |
| α-helix | 183-185 | 3 | |
| β-strand | 186 | 1 | 9 |
| β-strand | 197 | 1 | 9 |
| α-helix | 204-222 | 19 | |
| β-strand | 229-231 | 3 | 8 |
| 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 | 8 |
| α-helix | 285-287 | 3 | |
| α-helix | 290-296 | 7 | |
| α-helix | 299-302 | 4 | |
| β-strand | 307-311 | 5 | 8 |
| α-helix | 315-317 | 3 | |
| α-helix | 320 | 1 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-330 | 5 | |
| β-strand | 335-340 | 6 | 8 |
| α-helix | 357-372 | 16 | |
| β-strand | 375-382 | 8 | 8 |
| β-strand | 385 | 1 | 6 |
| β-strand | 402-405 | 4 | 6 |
| α-helix | 406-408 | 3 | |
| β-strand | 410-413 | 4 | 6 |
| α-helix | 415-424 | 10 | |
| β-strand | 432-438 | 7 | 7 |
| β-strand | 445-450 | 6 | 7 |
| β-strand | 456-462 | 7 | 7 |
| β-strand | 468-474 | 7 | 7 |
| β-strand | 478-484 | 7 | 7 |
| β-strand | 488-494 | 7 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysosomal acid glucosylceramidase | AAA, BBB | protein | 497 | Homo sapiens | P04062 (AlphaFold model) |
>6TJK_1 Lysosomal acid glucosylceramidase (chains AAA, BBB) 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 | 3 |
| B3P | 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-pr… | C11 H26 N2 O6 | 2 |
Water and common crystallization additives (SO4, EDO) are not listed.
A baculoviral system for the production of human beta-glucocerebrosidase enables atomic resolution analysis. Rowland, R.J., Wu, L., Liu, F. et al. Acta Crystallogr D Struct Biol (2020) 76:565-580. DOI 10.1107/S205979832000501X · 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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