Crystal structure of RBBP4 in complex with PRDM3 N-terminal peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 27 Dec 2017.
Explore 6BW3 in 3D Show helices and sheets RCSB PDB PDBe
6BW3 contains 11 α-helices and 60 β-strands across 3 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 | 10-31 | 22 | |
| 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 | 129-133 | 5 | 10 |
| β-strand | 136-143 | 8 | 10 |
| β-strand | 149-153 | 5 | 10 |
| α-helix | 154-156 | 3 | |
| α-helix | 161-162 | 2 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-31 | 19 | |
| 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 | 129-133 | 5 | 3 |
| β-strand | 136-143 | 8 | 3 |
| β-strand | 149-153 | 5 | 3 |
| α-helix | 154-156 | 3 | |
| α-helix | 161-162 | 2 | |
| β-strand | 171-174 | 4 | 3 |
| β-strand | 183-185 | 3 | 4 |
| β-strand | 192-196 | 5 | 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-binding protein RBBP4 | A, C | protein | 427 | Homo sapiens | Q09028 (AlphaFold model) |
| MDS1 and EVI1 complex locus protein MDS1 | B, D | protein | 12 | Homo sapiens | Q03112 (AlphaFold model) |
>6BW3_1 Histone-binding protein RBBP4 (chains A, C) GSMADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEG KDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIE IKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQK EGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLL HESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTV ALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPED AEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGSV DPEGQGS
>6BW3_2 MDS1 and EVI1 complex locus protein MDS1 (chains B, D) MRSKGRARKLAT
Direct interaction between the PRDM3 and PRDM16 tumor suppressors and the NuRD chromatin remodeling complex. Ivanochko, D., Halabelian, L., Henderson, E. et al. Nucleic Acids Res (2019) 47:1225-1238. DOI 10.1093/nar/gky1192 · 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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