Crystal structure of Rsa4 from Saccharomyces cerevisiae. Determined by X-ray diffraction at 2.8 Å resolution. Released 19 Nov 2014.
Explore 4WJU in 3D Show helices and sheets RCSB PDB PDBe
4WJU contains 22 α-helices and 83 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 | 34-38 | 5 | 1 |
| β-strand | 43 | 1 | 1 |
| β-strand | 49-50 | 2 | 1 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-80 | 4 | 1 |
| α-helix | 103-105 | 3 | |
| β-strand | 117-123 | 7 | 1 |
| α-helix | 129-132 | 4 | |
| β-strand | 134-135 | 2 | 2 |
| α-helix | 137-138 | 2 | |
| β-strand | 139 | 1 | 2 |
| α-helix | 140 | 1 | |
| β-strand | 146-151 | 6 | 3 |
| β-strand | 158-163 | 6 | 3 |
| β-strand | 168-172 | 5 | 3 |
| β-strand | 177-182 | 6 | 3 |
| β-strand | 189-194 | 6 | 4 |
| β-strand | 201-205 | 5 | 4 |
| β-strand | 210-213 | 4 | 4 |
| β-strand | 220 | 1 | 4 |
| β-strand | 225 | 1 | 4 |
| β-strand | 232-237 | 6 | 5 |
| α-helix | 238-239 | 2 | |
| α-helix | 240-242 | 3 | |
| α-helix | 244 | 1 | |
| β-strand | 245 | 1 | 6 |
| β-strand | 247 | 1 | 6 |
| β-strand | 251-255 | 5 | 5 |
| β-strand | 260-264 | 5 | 5 |
| β-strand | 269-273 | 5 | 5 |
| β-strand | 281-286 | 6 | 7 |
| β-strand | 291-296 | 6 | 7 |
| β-strand | 301-305 | 5 | 7 |
| α-helix | 306-308 | 3 | |
| β-strand | 311-316 | 6 | 7 |
| β-strand | 323-328 | 6 | 8 |
| α-helix | 331-336 | 6 | |
| α-helix | 344-346 | 3 | |
| α-helix | 349-364 | 16 | |
| β-strand | 365 | 1 | 9 |
| β-strand | 370 | 1 | 9 |
| β-strand | 374-378 | 5 | 8 |
| β-strand | 383-386 | 4 | 8 |
| β-strand | 396-398 | 3 | 8 |
| β-strand | 405-410 | 6 | 10 |
| β-strand | 416-421 | 6 | 10 |
| β-strand | 426-430 | 5 | 10 |
| β-strand | 436-440 | 5 | 10 |
| β-strand | 447-452 | 6 | 11 |
| β-strand | 458-463 | 6 | 11 |
| β-strand | 467-472 | 6 | 11 |
| β-strand | 477-483 | 7 | 11 |
| β-strand | 489-494 | 6 | 2 |
| β-strand | 500-505 | 6 | 2 |
| β-strand | 510-514 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-38 | 5 | 12 |
| α-helix | 58-66 | 9 | |
| β-strand | 77-79 | 3 | 12 |
| α-helix | 101-105 | 5 | |
| β-strand | 117-123 | 7 | 12 |
| α-helix | 129-132 | 4 | |
| β-strand | 134-140 | 7 | 13 |
| β-strand | 146-151 | 6 | 14 |
| β-strand | 158-163 | 6 | 14 |
| β-strand | 168-172 | 5 | 14 |
| β-strand | 177-182 | 6 | 14 |
| β-strand | 189-194 | 6 | 15 |
| β-strand | 201-205 | 5 | 15 |
| β-strand | 210-214 | 5 | 15 |
| β-strand | 219-220 | 2 | 15 |
| β-strand | 225 | 1 | 15 |
| β-strand | 232-237 | 6 | 16 |
| α-helix | 238-239 | 2 | |
| α-helix | 240-242 | 3 | |
| α-helix | 244 | 1 | |
| β-strand | 245 | 1 | 17 |
| β-strand | 247 | 1 | 17 |
| β-strand | 251-255 | 5 | 16 |
| β-strand | 259-263 | 5 | 16 |
| β-strand | 270-275 | 6 | 16 |
| β-strand | 281-286 | 6 | 18 |
| β-strand | 291-296 | 6 | 18 |
| β-strand | 301-305 | 5 | 18 |
| α-helix | 306-308 | 3 | |
| β-strand | 311-316 | 6 | 18 |
| β-strand | 323-328 | 6 | 19 |
| α-helix | 331-336 | 6 | |
| α-helix | 344-346 | 3 | |
| α-helix | 349-364 | 16 | |
| β-strand | 365 | 1 | 20 |
| β-strand | 370 | 1 | 20 |
| β-strand | 374-378 | 5 | 19 |
| β-strand | 383-387 | 5 | 19 |
| β-strand | 391-396 | 6 | 19 |
| β-strand | 405-410 | 6 | 21 |
| β-strand | 416-421 | 6 | 21 |
| β-strand | 426-430 | 5 | 21 |
| β-strand | 436-440 | 5 | 21 |
| β-strand | 447-452 | 6 | 22 |
| β-strand | 458-463 | 6 | 22 |
| β-strand | 467-472 | 6 | 22 |
| β-strand | 477-483 | 7 | 22 |
| β-strand | 489-494 | 6 | 13 |
| β-strand | 500-505 | 6 | 13 |
| β-strand | 509-514 | 6 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribosome assembly protein 4 | A, B | protein | 515 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P25382 (AlphaFold model) |
>4WJU_1 Ribosome assembly protein 4 (chains A, B) MSTLIPPPSKKQKKEAQLPREVAIIPKDLPNVSIKFQALDTGDNVGGALRVPGAISEKQL EELLNQLNGTSDDPVPYTFSCTIQGKKASDPVKTIDITDNLYSSLIKPGYNSTEDQITLL YTPRAVFKVKPVTRSSSAIAGHGSTILCSAFAPHTSSRMVTGAGDNTARIWDCDTQTPMH TLKGHYNWVLCVSWSPDGEVIATGSMDNTIRLWDPKSGQCLGDALRGHSKWITSLSWEPI HLVKPGSKPRLASSSKDGTIKIWDTVSRVCQYTMSGHTNSVSCVKWGGQGLLYSGSHDRT VRVWDINSQGRCINILKSHAHWVNHLSLSTDYALRIGAFDHTGKKPSTPEEAQKKALENY EKICKKNGNSEEMMVTASDDYTMFLWNPLKSTKPIARMTGHQKLVNHVAFSPDGRYIVSA SFDNSIKLWDGRDGKFISTFRGHVASVYQVAWSSDCRLLVSCSKDTTLKVWDVRTRKLSV DLPGHKDEVYTVDWSVDGKRVCSGGKDKMVRLWTH
A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. Baler, J., Paternoga, H., Holdermann, I. et al. J Cell Biol (2014) 207:481-498. DOI 10.1083/jcb.201408111 · PubMed
Other PDB entries of the same protein (UniProt P25382 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4WJU 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.