Cryo-EM structure of C-mannosyltransferase CeDPY19, in complex with Dol25-P-Man and bound to CMT2-Fab and anti-Fab nanobody. Determined by electron microscopy at 2.99 Å resolution. Released 11 Jan 2023.
Explore 7ZLI in 3D Show helices and sheets RCSB PDB PDBe
7ZLI contains 49 α-helices and 65 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 | 26-54 | 29 | |
| α-helix | 56-58 | 3 | |
| α-helix | 61-67 | 7 | |
| α-helix | 72-84 | 13 | |
| α-helix | 88-96 | 9 | |
| β-strand | 98 | 1 | 15 |
| β-strand | 107 | 1 | 15 |
| α-helix | 110-113 | 4 | |
| α-helix | 116-135 | 20 | |
| β-strand | 140-145 | 6 | 16 |
| α-helix | 151-152 | 2 | |
| β-strand | 153-158 | 6 | 16 |
| α-helix | 162-174 | 13 | |
| α-helix | 177-189 | 13 | |
| α-helix | 192-204 | 13 | |
| α-helix | 220-239 | 20 | |
| α-helix | 245-260 | 16 | |
| α-helix | 265-280 | 16 | |
| α-helix | 287-307 | 21 | |
| α-helix | 319-331 | 13 | |
| α-helix | 334-336 | 3 | |
| β-strand | 341 | 1 | 17 |
| α-helix | 342-362 | 21 | |
| α-helix | 364-369 | 6 | |
| α-helix | 375-378 | 4 | |
| α-helix | 381-384 | 4 | |
| α-helix | 389-396 | 8 | |
| α-helix | 403-405 | 3 | |
| α-helix | 406-414 | 9 | |
| α-helix | 418-434 | 17 | |
| β-strand | 440 | 1 | 17 |
| α-helix | 450-468 | 19 | |
| α-helix | 473-484 | 12 | |
| α-helix | 485-488 | 4 | |
| α-helix | 500-526 | 27 | |
| α-helix | 535-547 | 13 | |
| β-strand | 554-556 | 3 | 18 |
| α-helix | 558-566 | 9 | |
| β-strand | 572 | 1 | 18 |
| α-helix | 586-591 | 6 | |
| α-helix | 592-594 | 3 | |
| α-helix | 599-609 | 11 | |
| β-strand | 613-617 | 5 | 18 |
| α-helix | 618-621 | 4 | |
| α-helix | 632-638 | 7 | |
| α-helix | 641-643 | 3 | |
| α-helix | 647-648 | 2 | |
| α-helix | 649-659 | 11 | |
| β-strand | 668-674 | 7 | 18 |
| β-strand | 678-683 | 6 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 1 |
| β-strand | 13-15 | 3 | 2 |
| β-strand | 20-28 | 9 | 1 |
| α-helix | 31 | 1 | |
| β-strand | 36-42 | 7 | 2 |
| β-strand | 48-55 | 8 | 2 |
| β-strand | 60-63 | 4 | 2 |
| β-strand | 71-76 | 6 | 1 |
| β-strand | 81-87 | 7 | 1 |
| β-strand | 95-102 | 8 | 2 |
| α-helix | 112-114 | 3 | |
| β-strand | 117-118 | 2 | 2 |
| β-strand | 122-126 | 5 | 2 |
| β-strand | 132 | 1 | 3 |
| β-strand | 135-139 | 5 | 4 |
| α-helix | 140-142 | 3 | |
| β-strand | 151-160 | 10 | 4 |
| β-strand | 161 | 1 | 3 |
| β-strand | 166-169 | 4 | 5 |
| α-helix | 170-172 | 3 | |
| β-strand | 178-180 | 3 | 4 |
| β-strand | 184-185 | 2 | 4 |
| β-strand | 191-199 | 9 | 4 |
| α-helix | 203-206 | 4 | |
| β-strand | 209-215 | 7 | 5 |
| β-strand | 220-226 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 6 |
| β-strand | 12 | 1 | 7 |
| β-strand | 18-25 | 8 | 6 |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 46-51 | 6 | 8 |
| β-strand | 58-60 | 3 | 8 |
| β-strand | 61 | 1 | 9 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 92-97 | 6 | 8 |
| β-strand | 98-99 | 2 | 10 |
| β-strand | 108-110 | 3 | 10 |
| β-strand | 115-117 | 3 | 8 |
| β-strand | 119 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 11 |
| β-strand | 11-14 | 4 | 12 |
| β-strand | 20-26 | 7 | 11 |
| β-strand | 34-39 | 6 | 12 |
| β-strand | 46-50 | 5 | 12 |
| β-strand | 54-55 | 2 | 12 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 11 |
| β-strand | 71-76 | 6 | 11 |
| β-strand | 86-91 | 6 | 12 |
| β-strand | 99 | 1 | 12 |
| β-strand | 103-107 | 5 | 12 |
| β-strand | 111 | 1 | 9 |
| β-strand | 115-119 | 5 | 13 |
| α-helix | 123-126 | 4 | |
| β-strand | 130-140 | 11 | 13 |
| β-strand | 147-150 | 4 | 14 |
| β-strand | 160-164 | 5 | 13 |
| α-helix | 165-168 | 4 | |
| β-strand | 174-183 | 10 | 13 |
| α-helix | 184-187 | 4 | |
| β-strand | 192-199 | 8 | 14 |
| β-strand | 202-211 | 10 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CMT2-Fab heavy chain | H | protein | 236 | synthetic construct | |
| Anti-Fab nanobody | K | protein | 123 | synthetic construct | |
| CMT2-Fab light chain | L | protein | 215 | synthetic construct | Q7Z3Y4 (AlphaFold model) |
| C-mannosyltransferase dpy-19 | A | protein | 707 | Caenorhabditis elegans | P34413 (AlphaFold model) |
>7ZLI_1 CMT2-Fab heavy chain (chains H) EISEVQLVESGGGLVQPGGSLRLSCAASGFNISSSSIHWVRQAPGKGLEWVASISSSYGY TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSSSVYWSWWGYSAFDYWGQ GTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHT FPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
>7ZLI_2 Anti-Fab nanobody (chains K) GSQVQLQESGGGLVQPGGSLRLSCAASGRTISRYAMSWFRQAPGKEREFVAVARRSGDGA FYADSVQGRFTVSRDDAKNTVYLQMNSLKPEDTAVYYCAIDSDTFYSGSYDYWGQGTQVT VSS
>7ZLI_3 CMT2-Fab light chain (chains L) SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP SRFSGSRSGTDFTLTISSLQPEDFATYYCQQGASEPITFGQGTKVEIKRTVAAPSVFIFP PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>7ZLI_4 C-mannosyltransferase dpy-19 (chains A) MAKKPKNSPEKSKYSSDTSSSLYSQTWLASVVIIGLLVGYINYQHVYTLFENDKHFSHLA DFEREMAYRTEMGLYYSYYKTIINAPSFLEGVQEITHDTVTEHGHEINTLNRFNLYPEVI LAFLYRPFRAFAKSANWQIELCWQVNRGELRPVESCEGIGNPHYFYITGVFIVAGTVASS IFYLGVLVSDSIFGGFLSVLCFAFNHGEATRVQWTPPLRESFAFPFIIGHIAILTFVIKY KKSGHSMILLLTSMAVPALLFWQFTQFAFFTQICSIFLAFSLDLIPFSTAKTVIHSHIIS FLIGFLLLFGNEMMITALYFPSILALGMIIYISPLLSNLKFRPAYVLFLAIIFASITLGL KIGLSKGLGIEDDAHIFDILRSKFTSFANFHTRLYTCSAEFDFIQYSTIEKLCGTLLIPL ALISLVTFVFNFVKNTNLLWRNSEEIGENGEILYNVVQLCCSTVMAFLIMRLKLFMTPHL CIVAALFANSKLLGGDRISKTIRVSALVGVIAILFYRGIPNIRQQLNVKGEYSNPDQEML FDWIQHNTKQDAVFAGTMPVMANVKLTTLRPIVNHPHYEHVGIRERTLKVYSMFSKKPIA EVHKIMKEMGVNYFVFQLMNCSNDERRPECVYRGMWDEEDPKNSGRTALCDLWILAANSK DNSRIAPFKIVYNANRNYIVLKILEDYKDHDGDYKDHDIDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| IZY | Dolichol monophosphate beta-D-Mannose | C31 H55 O9 P | 1 |
Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase. Bloch, J.S., John, A., Mao, R. et al. Nat Chem Biol (2023) 19:575-584. DOI 10.1038/s41589-022-01219-9 · PubMed
Other PDB entries of the same protein (UniProt Q7Z3Y4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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