Structure of Cerezyme at pH 4.6. Determined by X-ray diffraction at 1.59 Å resolution. Released 10 Jun 2020.
Explore 6TJJ in 3D Show helices and sheets RCSB PDB PDBe
6TJJ contains 47 α-helices and 56 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 | 6-7 | 2 | 2 |
| β-strand | 15-18 | 4 | 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 |
| 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 | 196 | 1 | 6 |
| β-strand | 197 | 1 | 5 |
| α-helix | 204-222 | 19 | |
| β-strand | 229-231 | 3 | 4 |
| α-helix | 236-240 | 5 | |
| β-strand | 250 | 1 | 6 |
| 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 | 320 | 1 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-330 | 5 | |
| β-strand | 335-342 | 8 | 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 7 |
| β-strand | 6-7 | 2 | 8 |
| β-strand | 15-18 | 4 | 8 |
| β-strand | 25 | 1 | 7 |
| α-helix | 27 | 1 | |
| α-helix | 29 | 1 | |
| β-strand | 36-42 | 7 | 9 |
| β-strand | 50-55 | 6 | 9 |
| β-strand | 57 | 1 | 9 |
| β-strand | 65-77 | 13 | 9 |
| α-helix | 78 | 1 | |
| β-strand | 80-84 | 5 | 10 |
| α-helix | 87-94 | 8 | |
| α-helix | 98-109 | 12 | |
| β-strand | 118-123 | 6 | 10 |
| α-helix | 151 | 1 | |
| α-helix | 152-157 | 6 | |
| α-helix | 158-167 | 10 | |
| α-helix | 171-172 | 2 | |
| β-strand | 173-178 | 6 | 10 |
| α-helix | 183-185 | 3 | |
| β-strand | 186 | 1 | 11 |
| β-strand | 197 | 1 | 11 |
| α-helix | 204-222 | 19 | |
| β-strand | 229-231 | 3 | 10 |
| α-helix | 236-240 | 5 | |
| α-helix | 253-259 | 7 | |
| α-helix | 260-264 | 5 | |
| α-helix | 265-270 | 6 | |
| β-strand | 277-284 | 8 | 10 |
| α-helix | 285-287 | 3 | |
| α-helix | 290-296 | 7 | |
| α-helix | 299-302 | 4 | |
| β-strand | 307-313 | 7 | 10 |
| α-helix | 321-325 | 5 | |
| α-helix | 326-330 | 5 | |
| β-strand | 335-342 | 8 | 10 |
| α-helix | 357-372 | 16 | |
| β-strand | 375-382 | 8 | 10 |
| β-strand | 385 | 1 | 8 |
| β-strand | 402-405 | 4 | 8 |
| α-helix | 406-408 | 3 | |
| β-strand | 410-413 | 4 | 8 |
| α-helix | 415-424 | 10 | |
| β-strand | 432-438 | 7 | 9 |
| β-strand | 444-450 | 7 | 9 |
| β-strand | 456-462 | 7 | 9 |
| β-strand | 468-474 | 7 | 9 |
| β-strand | 478-484 | 7 | 9 |
| β-strand | 489-494 | 6 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucosylceramidase | AAA, BBB | protein | 497 | Homo sapiens | P04062 (AlphaFold model) |
>6TJJ_1 Glucosylceramidase (chains AAA, BBB) ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANH TGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIR VPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWT SPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGL LSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPE AAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRG MQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHL GHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFL ETISPGYSIHTYLWHRQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (SO4, ACT, K, NA) 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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