Single-chain human APRIL-BAFF-BAFF Heterotrimer. Determined by X-ray diffraction at 2.43 Å resolution. Released 13 May 2015.
Explore 4ZCH in 3D Show helices and sheets RCSB PDB PDBe
4ZCH contains 10 α-helices and 76 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 | 9-18 | 10 | 1 |
| β-strand | 26-36 | 11 | 1 |
| β-strand | 40-42 | 3 | 1 |
| β-strand | 47-49 | 3 | 1 |
| β-strand | 53-63 | 11 | 1 |
| β-strand | 69-77 | 9 | 1 |
| β-strand | 82-91 | 10 | 1 |
| β-strand | 101-111 | 11 | 1 |
| β-strand | 116-121 | 6 | 1 |
| β-strand | 128-129 | 2 | 1 |
| β-strand | 136-141 | 6 | 1 |
| β-strand | 154-159 | 6 | 2 |
| α-helix | 164-165 | 2 | |
| β-strand | 166-168 | 3 | 3 |
| β-strand | 171-173 | 3 | 3 |
| β-strand | 176-182 | 7 | 2 |
| β-strand | 186-189 | 4 | 3 |
| β-strand | 192-195 | 4 | 3 |
| β-strand | 199-209 | 11 | 2 |
| β-strand | 215-223 | 9 | 3 |
| β-strand | 234-243 | 10 | 3 |
| β-strand | 251-261 | 11 | 2 |
| β-strand | 266-271 | 6 | 3 |
| β-strand | 278 | 1 | 2 |
| β-strand | 286-291 | 6 | 2 |
| α-helix | 292-293 | 2 | |
| β-strand | 305-310 | 6 | 4 |
| α-helix | 315-316 | 2 | |
| β-strand | 317-319 | 3 | 5 |
| β-strand | 322-324 | 3 | 5 |
| α-helix | 325-326 | 2 | |
| β-strand | 327-333 | 7 | 4 |
| β-strand | 337-340 | 4 | 5 |
| β-strand | 343-346 | 4 | 5 |
| β-strand | 350-360 | 11 | 4 |
| β-strand | 366-377 | 12 | 5 |
| β-strand | 382-394 | 13 | 5 |
| β-strand | 402-412 | 11 | 4 |
| β-strand | 417-422 | 6 | 5 |
| β-strand | 429 | 1 | 4 |
| β-strand | 437-443 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-18 | 10 | 6 |
| β-strand | 26-36 | 11 | 6 |
| β-strand | 40-44 | 5 | 6 |
| β-strand | 46-49 | 4 | 6 |
| β-strand | 53-63 | 11 | 6 |
| α-helix | 69 | 1 | |
| β-strand | 70 | 1 | 7 |
| β-strand | 73-78 | 6 | 6 |
| β-strand | 81-87 | 7 | 6 |
| β-strand | 90 | 1 | 7 |
| β-strand | 101-111 | 11 | 6 |
| β-strand | 116-121 | 6 | 6 |
| β-strand | 128 | 1 | 6 |
| β-strand | 136-141 | 6 | 6 |
| β-strand | 154-159 | 6 | 8 |
| α-helix | 164-165 | 2 | |
| β-strand | 166-168 | 3 | 9 |
| β-strand | 171-173 | 3 | 9 |
| α-helix | 174-175 | 2 | |
| β-strand | 176-182 | 7 | 8 |
| β-strand | 186-189 | 4 | 9 |
| β-strand | 192-195 | 4 | 9 |
| β-strand | 199-209 | 11 | 8 |
| β-strand | 215-223 | 9 | 9 |
| β-strand | 234-243 | 10 | 9 |
| β-strand | 251-261 | 11 | 8 |
| β-strand | 266-271 | 6 | 9 |
| β-strand | 278 | 1 | 8 |
| β-strand | 286-291 | 6 | 8 |
| α-helix | 292-293 | 2 | |
| β-strand | 305-310 | 6 | 10 |
| α-helix | 315-316 | 2 | |
| β-strand | 317-318 | 2 | 11 |
| β-strand | 323-324 | 2 | 11 |
| α-helix | 325-326 | 2 | |
| β-strand | 327-333 | 7 | 10 |
| β-strand | 337-340 | 4 | 11 |
| β-strand | 343-346 | 4 | 11 |
| β-strand | 350-360 | 11 | 10 |
| β-strand | 366-377 | 12 | 11 |
| β-strand | 382-394 | 13 | 11 |
| β-strand | 402-412 | 11 | 10 |
| β-strand | 417-422 | 6 | 11 |
| β-strand | 429-430 | 2 | 10 |
| β-strand | 437-442 | 6 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tumor necrosis factor ligand superfamily member 13,Tumor necrosis factor ligand superfamily member… | A, B | protein | 438 | Homo sapiens | O75888 (AlphaFold model), Q9Y275 (AlphaFold model) |
>4ZCH_1 Tumor necrosis factor ligand superfamily member 13,Tumor necrosis factor ligand superfamily member 13B,Tumor necrosis factor ligand superfamily member 13B (chains A, B) HSVLHLVPINAASKDDSDVTEVMWQPALRRGRGLQAQGYGVRIQDAGVYLLYSQVLFQDV TFTMGQVVSREGQGRQETLFRCIRSMPSHPDRAYNSCYSAGVFHLHQGDILSVIIPRARA KLNLSPHGTFLGFVKLGGGGSETVTQDCLQLIADSETPTIQKGSYTFVPWLLSFKRGSAL EEKENKILVKETGYFFIYGQVLYTDKTYAMGHLIQRKKVHVFGDELSLVTLFRCIQNMPE TLPNNSCYSAGIAKLEEGDELQLAIPRENAQISLDGDVTFFGALKLLGGGGSETVTQDCL QLIADSETPTIQKGSYTFVPWLLSFKRGSALEEKENKILVKETGYFFIYGQVLYTDKTYA MGHLIQRKKVHVFGDELSLVTLFRCIQNMPETLPNNSCYSAGIAKLEEGDELQLAIPREN AQISLDGDVTFFGALKLL
| ID | Name | Formula | Copies |
|---|---|---|---|
| 144 | Tris-hydroxymethyl-methyl-ammonium | C4 H12 N O3 | 1 |
Stoichiometry of Heteromeric BAFF and APRIL Cytokines Dictates Their Receptor Binding and Signaling Properties. Schuepbach-Mallepell, S., Das, D., Willen, L. et al. J Biol Chem (2015) 290:16330-16342. DOI 10.1074/jbc.M115.661405 · PubMed
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