Crystal structure of MBP fused GAS41 YEATS domain in complex with H3K27ac peptide. Determined by X-ray diffraction at 2.1 Å resolution. Released 1 Nov 2023.
Explore 8IIZ in 3D Show helices and sheets RCSB PDB PDBe
8IIZ contains 31 α-helices and 37 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 | -350--349 | 2 | |
| β-strand | -346--342 | 5 | 1 |
| α-helix | -335--321 | 15 | |
| β-strand | -318--314 | 5 | 1 |
| α-helix | -309--301 | 9 | |
| β-strand | -293--289 | 5 | 1 |
| α-helix | -288--286 | 3 | |
| α-helix | -285--280 | 6 | |
| β-strand | -276 | 1 | 2 |
| α-helix | -275--273 | 3 | |
| α-helix | -269--266 | 4 | |
| β-strand | -263 | 1 | 3 |
| α-helix | -261--256 | 6 | |
| β-strand | -254--253 | 2 | 4 |
| β-strand | -250--249 | 2 | 4 |
| β-strand | -246--241 | 6 | 1 |
| β-strand | -238--234 | 5 | 5 |
| β-strand | -224 | 1 | 6 |
| α-helix | -220--212 | 9 | |
| β-strand | -207 | 1 | 7 |
| α-helix | -198--189 | 10 | |
| β-strand | -185--180 | 6 | 8 |
| β-strand | -177--170 | 8 | 8 |
| α-helix | -166--152 | 15 | |
| α-helix | -142--134 | 9 | |
| β-strand | -130 | 1 | 7 |
| β-strand | -128--125 | 4 | 5 |
| α-helix | -123--121 | 3 | |
| α-helix | -120--115 | 6 | |
| β-strand | -110--107 | 4 | 5 |
| α-helix | -106--104 | 3 | |
| β-strand | -103 | 1 | 6 |
| β-strand | -102 | 1 | 9 |
| β-strand | -99 | 1 | 9 |
| α-helix | -98--97 | 2 | |
| α-helix | -95 | 1 | |
| β-strand | -94--93 | 2 | 10 |
| β-strand | -92--86 | 7 | 1 |
| β-strand | -85 | 1 | 2 |
| α-helix | -79--74 | 6 | |
| α-helix | -73--68 | 6 | |
| α-helix | -65--58 | 8 | |
| β-strand | -51--50 | 2 | 1 |
| β-strand | -48 | 1 | 3 |
| α-helix | -47--41 | 7 | |
| α-helix | -37--26 | 12 | |
| β-strand | -24--23 | 2 | 10 |
| α-helix | -22--21 | 2 | |
| α-helix | -16--1 | 16 | |
| α-helix | 5-17 | 13 | |
| β-strand | 20-33 | 14 | 11 |
| α-helix | 34 | 1 | |
| β-strand | 45-53 | 9 | 11 |
| α-helix | 59-61 | 3 | |
| β-strand | 63-69 | 7 | 12 |
| β-strand | 78-81 | 4 | 12 |
| β-strand | 86-92 | 7 | 11 |
| β-strand | 95 | 1 | 13 |
| β-strand | 97-104 | 8 | 12 |
| α-helix | 110-111 | 2 | |
| β-strand | 112-117 | 6 | 12 |
| α-helix | 133 | 1 | |
| β-strand | 134-145 | 12 | 11 |
| α-helix | 149-154 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 11 |
| α-helix | 7-8 | 2 | |
| β-strand | 9-10 | 2 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28 | 1 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltodextrin-binding protein,YEATS domain-containing protein 4 | A | protein | 514 | Escherichia coli, Homo sapiens | O95619 (AlphaFold model), P0AEX9 (AlphaFold model) |
| Histone H3.1 | B, C | protein | 32 | Homo sapiens | P68431 (AlphaFold model) |
>8IIZ_1 Maltodextrin-binding protein,YEATS domain-containing protein 4 (chains A) GSMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP DIIFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYD IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT SAVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV DEALKDAQTNAAAVTIVKPIVYGNVARYFGKKREEDGHTHQWTVYVKPYRNEDMSAYVKK IQFKLHESYGNPLRVVTKPPYEITETGWGEFEIIIKIFFIDPNERPVTLYHLLKLFQSDT NAMLGKKTVVSEFYDEMIFQDPTAMMQQLLTTSR
>8IIZ_2 Histone H3.1 (chains B, C) ARTKQTARKSTGGKAPRKQLATKAARKSAPAT
GAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain. Kikuchi, M., Takase, S., Konuma, T. et al. Proc Natl Acad Sci U S A (2023) 120:e2304103120-e2304103120. DOI 10.1073/pnas.2304103120 · PubMed
Other PDB entries of the same protein (UniProt O95619 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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