7ZLI: C-mannosyltransferase CeDPY19

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.

Method
Electron microscopy
Resolution
2.99 Å
Organisms
synthetic construct, Caenorhabditis elegans
Chains
4
Atoms
9,582
Mol. weight
143.13 kDa
Ligands
IZY
Released
11 Jan 2023

Explore 7ZLI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 39 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix26-5429
α-helix56-583
α-helix61-677
α-helix72-8413
α-helix88-969
β-strand98115
β-strand107115
α-helix110-1134
α-helix116-13520
β-strand140-145616
α-helix151-1522
β-strand153-158616
α-helix162-17413
α-helix177-18913
α-helix192-20413
α-helix220-23920
α-helix245-26016
α-helix265-28016
α-helix287-30721
α-helix319-33113
α-helix334-3363
β-strand341117
α-helix342-36221
α-helix364-3696
α-helix375-3784
α-helix381-3844
α-helix389-3968
α-helix403-4053
α-helix406-4149
α-helix418-43417
β-strand440117
α-helix450-46819
α-helix473-48412
α-helix485-4884
α-helix500-52627
α-helix535-54713
β-strand554-556318
α-helix558-5669
β-strand572118
α-helix586-5916
α-helix592-5943
α-helix599-60911
β-strand613-617518
α-helix618-6214
α-helix632-6387
α-helix641-6433
α-helix647-6482
α-helix649-65911
β-strand668-674718
β-strand678-683618
Chain H: 5 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand6-1051
β-strand13-1532
β-strand20-2891
α-helix311
β-strand36-4272
β-strand48-5582
β-strand60-6342
β-strand71-7661
β-strand81-8771
β-strand95-10282
α-helix112-1143
β-strand117-11822
β-strand122-12652
β-strand13213
β-strand135-13954
α-helix140-1423
β-strand151-160104
β-strand16113
β-strand166-16945
α-helix170-1723
β-strand178-18034
β-strand184-18524
β-strand191-19994
α-helix203-2064
β-strand209-21575
β-strand220-22675
Chain K: 1 helix, 14 β-strands
ElementResiduesLengthSheet
β-strand3-646
β-strand1217
β-strand18-2586
β-strand34-3968
β-strand46-5168
β-strand58-6038
β-strand6119
α-helix62-643
β-strand68-7366
β-strand78-8366
β-strand92-9768
β-strand98-99210
β-strand108-110310
β-strand115-11738
β-strand11917
Chain L: 4 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand5-7311
β-strand11-14412
β-strand20-26711
β-strand34-39612
β-strand46-50512
β-strand54-55212
α-helix561
β-strand63-68611
β-strand71-76611
β-strand86-91612
β-strand99112
β-strand103-107512
β-strand11119
β-strand115-119513
α-helix123-1264
β-strand130-1401113
β-strand147-150414
β-strand160-164513
α-helix165-1684
β-strand174-1831013
α-helix184-1874
β-strand192-199814
β-strand202-2111014

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CMT2-Fab heavy chainHprotein236synthetic construct
Anti-Fab nanobodyKprotein123synthetic construct
CMT2-Fab light chainLprotein215synthetic constructQ7Z3Y4 (AlphaFold model)
C-mannosyltransferase dpy-19Aprotein707Caenorhabditis elegansP34413 (AlphaFold model)
Sequence of entity 1 (H), FASTA
>7ZLI_1 CMT2-Fab heavy chain (chains H)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNISSSSIHWVRQAPGKGLEWVASISSSYGY
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSSSVYWSWWGYSAFDYWGQ
GTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHT
FPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
Sequence of entity 2 (K), FASTA
>7ZLI_2 Anti-Fab nanobody (chains K)
GSQVQLQESGGGLVQPGGSLRLSCAASGRTISRYAMSWFRQAPGKEREFVAVARRSGDGA
FYADSVQGRFTVSRDDAKNTVYLQMNSLKPEDTAVYYCAIDSDTFYSGSYDYWGQGTQVT
VSS
Sequence of entity 3 (L), FASTA
>7ZLI_3 CMT2-Fab light chain (chains L)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQGASEPITFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 4 (A), FASTA
>7ZLI_4 C-mannosyltransferase dpy-19 (chains A)
MAKKPKNSPEKSKYSSDTSSSLYSQTWLASVVIIGLLVGYINYQHVYTLFENDKHFSHLA
DFEREMAYRTEMGLYYSYYKTIINAPSFLEGVQEITHDTVTEHGHEINTLNRFNLYPEVI
LAFLYRPFRAFAKSANWQIELCWQVNRGELRPVESCEGIGNPHYFYITGVFIVAGTVASS
IFYLGVLVSDSIFGGFLSVLCFAFNHGEATRVQWTPPLRESFAFPFIIGHIAILTFVIKY
KKSGHSMILLLTSMAVPALLFWQFTQFAFFTQICSIFLAFSLDLIPFSTAKTVIHSHIIS
FLIGFLLLFGNEMMITALYFPSILALGMIIYISPLLSNLKFRPAYVLFLAIIFASITLGL
KIGLSKGLGIEDDAHIFDILRSKFTSFANFHTRLYTCSAEFDFIQYSTIEKLCGTLLIPL
ALISLVTFVFNFVKNTNLLWRNSEEIGENGEILYNVVQLCCSTVMAFLIMRLKLFMTPHL
CIVAALFANSKLLGGDRISKTIRVSALVGVIAILFYRGIPNIRQQLNVKGEYSNPDQEML
FDWIQHNTKQDAVFAGTMPVMANVKLTTLRPIVNHPHYEHVGIRERTLKVYSMFSKKPIA
EVHKIMKEMGVNYFVFQLMNCSNDERRPECVYRGMWDEEDPKNSGRTALCDLWILAANSK
DNSRIAPFKIVYNANRNYIVLKILEDYKDHDGDYKDHDIDYKDDDDK

Ligands and cofactors

IDNameFormulaCopies
IZYDolichol monophosphate beta-D-MannoseC31 H55 O9 P1

Primary citation

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:

Browse structure collections

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