Crystal Structure of RBBP4-peptide complex. Determined by X-ray diffraction at 2.69 Å resolution. Released 11 Jul 2018.
Explore 5XWR in 3D Show helices and sheets RCSB PDB PDBe
5XWR contains 10 α-helices and 60 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 |
|---|---|---|---|
| α-helix | 16-27 | 12 | |
| α-helix | 28-30 | 3 | |
| β-strand | 32-39 | 8 | 1 |
| β-strand | 47-49 | 3 | 2 |
| β-strand | 54 | 1 | 2 |
| β-strand | 61-69 | 9 | 2 |
| β-strand | 77-87 | 11 | 2 |
| β-strand | 115-123 | 9 | 2 |
| β-strand | 130-132 | 3 | 3 |
| β-strand | 139-143 | 5 | 3 |
| β-strand | 149-153 | 5 | 3 |
| α-helix | 154-156 | 3 | |
| β-strand | 171-174 | 4 | 3 |
| β-strand | 180-185 | 6 | 4 |
| β-strand | 192-197 | 6 | 4 |
| β-strand | 202-206 | 5 | 4 |
| β-strand | 216-218 | 3 | 3 |
| β-strand | 221-223 | 3 | 4 |
| β-strand | 230-235 | 6 | 5 |
| β-strand | 242-247 | 6 | 5 |
| β-strand | 251-256 | 6 | 5 |
| β-strand | 267-270 | 4 | 5 |
| β-strand | 276-281 | 6 | 6 |
| β-strand | 288-293 | 6 | 6 |
| β-strand | 297-302 | 6 | 6 |
| β-strand | 311-314 | 4 | 6 |
| β-strand | 320-325 | 6 | 7 |
| β-strand | 332-337 | 6 | 7 |
| β-strand | 342-346 | 5 | 7 |
| α-helix | 347-349 | 3 | |
| β-strand | 366-370 | 5 | 7 |
| β-strand | 377-382 | 6 | 1 |
| β-strand | 389-394 | 6 | 1 |
| β-strand | 398-404 | 7 | 1 |
| α-helix | 406-409 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-27 | 12 | |
| α-helix | 28-30 | 3 | |
| β-strand | 32-39 | 8 | 8 |
| β-strand | 47-49 | 3 | 9 |
| β-strand | 54 | 1 | 9 |
| β-strand | 61-69 | 9 | 9 |
| β-strand | 77-87 | 11 | 9 |
| β-strand | 115-123 | 9 | 9 |
| β-strand | 129-132 | 4 | 10 |
| β-strand | 139-143 | 5 | 10 |
| β-strand | 149-153 | 5 | 10 |
| α-helix | 154-156 | 3 | |
| β-strand | 171-174 | 4 | 10 |
| β-strand | 183-185 | 3 | 11 |
| β-strand | 192-196 | 5 | 11 |
| β-strand | 202-206 | 5 | 11 |
| β-strand | 216-218 | 3 | 10 |
| β-strand | 221-223 | 3 | 11 |
| β-strand | 230-235 | 6 | 12 |
| β-strand | 242-247 | 6 | 12 |
| β-strand | 251-256 | 6 | 12 |
| β-strand | 267-270 | 4 | 12 |
| β-strand | 276-281 | 6 | 13 |
| β-strand | 288-293 | 6 | 13 |
| β-strand | 297-302 | 6 | 13 |
| β-strand | 311-314 | 4 | 13 |
| β-strand | 320-325 | 6 | 14 |
| β-strand | 332-337 | 6 | 14 |
| β-strand | 342-346 | 5 | 14 |
| α-helix | 347-349 | 3 | |
| β-strand | 366-370 | 5 | 14 |
| β-strand | 377-382 | 6 | 8 |
| β-strand | 389-394 | 6 | 8 |
| β-strand | 398-404 | 7 | 8 |
| α-helix | 406-409 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-binding protein RBBP4 | A, B | protein | 443 | Homo sapiens | Q09028 (AlphaFold model) |
| Met-ser-arg-arg-lys-gln-ala-lys-pro-gln-his-ile | C, D | protein | 12 | Homo sapiens | Q9UJQ4 (AlphaFold model) |
>5XWR_1 Histone-binding protein RBBP4 (chains A, B) HHHHHHHHHHLEVLFQGPMADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEW PSLTAQWLPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEK GEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPD PSGECNPDLRLRGHQKEGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTI FTGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFN PYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRL NVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVW QMAENIYNDEDPEGSVDPEGQGS
>5XWR_2 MET-SER-ARG-ARG-LYS-GLN-ALA-LYS-PRO-GLN-HIS-ILE (chains C, D) MSRRKQAKPQHI
Targeting cancer addiction for SALL4 by shifting its transcriptome with a pharmacologic peptide. Liu, B.H., Jobichen, C., Chia, C.S.B. et al. Proc Natl Acad Sci U S A (2018) 115:E7119-E7128. DOI 10.1073/pnas.1801253115 · PubMed
Other PDB entries of the same protein (UniProt Q09028 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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