CryoEM structure of tryptase in complex with engineered conformationally rigid anti-tryptase Fab E104.v1.4DS. Determined by electron microscopy at 2.5 Å resolution. Released 30 Oct 2024.
Explore 8VGJ in 3D Show helices and sheets RCSB PDB PDBe
8VGJ contains 90 α-helices and 284 β-strands across 12 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 | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| β-strand | 30-35 | 6 | 3 |
| β-strand | 39-48 | 10 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 60B | 1 | 4 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-67 | 4 | 3 |
| β-strand | 72 | 1 | 5 |
| β-strand | 83 | 1 | 3 |
| β-strand | 85-90 | 6 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 6 |
| β-strand | 118 | 1 | 6 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| β-strand | 136-140 | 5 | 2 |
| β-strand | 145 | 1 | 7 |
| β-strand | 149 | 1 | 7 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 5 |
| α-helix | 155 | 1 | |
| β-strand | 156-160 | 5 | 2 |
| β-strand | 162-163 | 2 | 2 |
| α-helix | 165-173 | 9 | |
| β-strand | 173C | 1 | 8 |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 185 | 1 | 9 |
| β-strand | 188 | 1 | 9 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-203 | 6 | 2 |
| β-strand | 206-215 | 10 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-238 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 19 |
| β-strand | 20-21 | 2 | 20 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 21 |
| β-strand | 39-48 | 10 | 21 |
| β-strand | 51-54 | 4 | 21 |
| α-helix | 56-58 | 3 | |
| β-strand | 60B | 1 | 17 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-67 | 4 | 21 |
| β-strand | 72 | 1 | 22 |
| β-strand | 83 | 1 | 21 |
| β-strand | 85-90 | 6 | 21 |
| β-strand | 104-108 | 5 | 21 |
| β-strand | 115 | 1 | 23 |
| β-strand | 118 | 1 | 23 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 20 |
| α-helix | 123-125 | 3 | |
| β-strand | 136-140 | 5 | 20 |
| β-strand | 145 | 1 | 24 |
| β-strand | 149 | 1 | 24 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 22 |
| α-helix | 155 | 1 | |
| β-strand | 156-160 | 5 | 20 |
| β-strand | 162-163 | 2 | 20 |
| α-helix | 165-173 | 9 | |
| β-strand | 173C | 1 | 13 |
| β-strand | 180-183 | 4 | 20 |
| β-strand | 185 | 1 | 25 |
| β-strand | 188 | 1 | 25 |
| β-strand | 189 | 1 | 19 |
| β-strand | 198-203 | 6 | 20 |
| β-strand | 206-215 | 10 | 20 |
| β-strand | 226-230 | 5 | 20 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-238 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 33 |
| β-strand | 10-14 | 5 | 34 |
| β-strand | 20-25 | 6 | 33 |
| β-strand | 33-38 | 6 | 34 |
| β-strand | 45-49 | 5 | 34 |
| β-strand | 53-54 | 2 | 34 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 33 |
| β-strand | 70-75 | 6 | 33 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-91 | 8 | 34 |
| β-strand | 96-98 | 3 | 34 |
| β-strand | 102-107 | 6 | 34 |
| β-strand | 111 | 1 | 35 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 36 |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 36 |
| β-strand | 140 | 1 | 35 |
| β-strand | 144-150 | 7 | 37 |
| β-strand | 153-154 | 2 | 37 |
| β-strand | 159-163 | 5 | 36 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 36 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 37 |
| β-strand | 205-210 | 6 | 37 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 38 |
| β-strand | 11-12 | 2 | 39 |
| β-strand | 18-24 | 7 | 38 |
| β-strand | 33-39 | 7 | 40 |
| β-strand | 46-51 | 6 | 40 |
| β-strand | 57-59 | 3 | 40 |
| α-helix | 63-65 | 3 | |
| β-strand | 67-72 | 6 | 38 |
| β-strand | 77-82 | 6 | 38 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 40 |
| β-strand | 102-103 | 2 | 40 |
| β-strand | 107-109 | 3 | 40 |
| β-strand | 110-111 | 2 | 39 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 41 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-128 | 5 | 42 |
| β-strand | 142-149 | 8 | 42 |
| β-strand | 150 | 1 | 41 |
| β-strand | 155-159 | 5 | 43 |
| α-helix | 160-162 | 3 | |
| β-strand | 169-170 | 2 | 42 |
| β-strand | 174-175 | 2 | 42 |
| β-strand | 181-187 | 7 | 42 |
| α-helix | 193-196 | 4 | |
| β-strand | 200-205 | 6 | 43 |
| α-helix | 206-208 | 3 | |
| β-strand | 210-215 | 6 | 43 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tryptase alpha/beta-1 | A, B, C, D | protein | 260 | Homo sapiens | Q15661 (AlphaFold model) |
| Fab E104.v1.4DS light chain | E, G, I, L | protein | 217 | Homo sapiens | |
| Fab E104.v1.4DS heavy chain | F, H, J, K | protein | 238 | Homo sapiens |
>8VGJ_1 Tryptase alpha/beta-1 (chains A, B, C, D) AGSTHHHHHHDDDDKIVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHC VGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSS HVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLG AYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPG IYTRVTYYLDWIHHYVPKKP
>8VGJ_2 Fab E104.v1.4DS light chain (chains E, G, I, L) DIQMTQSPSSLSASVGDRVTITCQSIKSVYNNRLGWYQQKCGKAPKLLIYETSILTSGVP SRFSGSGSGTDFTLTISSLQCEDFATYYCAGGFDRSGDTTFGQGTKVEIKRTVAAPSVFI FPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTCQDSKDCTYSLSS TLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>8VGJ_3 Fab E104.v1.4DS heavy chain (chains F, H, J, K) EVQLVESGPGCVKPSETLSLTCTVSRFSLIGYAITWIRQPPGKGLEWIGGISSAATTFYS SWAKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCARDPRGYGAALDRLDLWGQGTCVTV SSFSTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFCECPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTHHHHHHP
Disulfi de constrained Fabs overcome target size limitation for high-resolution single-particle cryo-EM. Kung, J.E., Johnson, M.C., Jao, C.C. et al. bioRxiv (2024). DOI 10.1101/2024.05.10.593593 · PubMed
Other PDB entries of the same protein (UniProt Q15661 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8VGJ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.