Complex Structure of Sgf29 and dimethylated H3K4. Determined by X-ray diffraction at 1.48 Å resolution. Released 4 May 2011.
Explore 3MP6 in 3D Show helices and sheets RCSB PDB PDBe
3MP6 contains 31 α-helices and 38 β-strands across 1 chain. 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 | 745-748 | 4 | 1 |
| α-helix | 755-769 | 15 | |
| β-strand | 773-776 | 4 | 1 |
| α-helix | 781-790 | 10 | |
| β-strand | 797-801 | 5 | 1 |
| α-helix | 802-804 | 3 | |
| α-helix | 805-810 | 6 | |
| β-strand | 814 | 1 | 2 |
| α-helix | 815-817 | 3 | |
| α-helix | 821-825 | 5 | |
| β-strand | 827 | 1 | 3 |
| α-helix | 829-834 | 6 | |
| β-strand | 836-837 | 2 | 4 |
| β-strand | 840-841 | 2 | 4 |
| β-strand | 844-849 | 6 | 1 |
| β-strand | 852-856 | 5 | 5 |
| β-strand | 866 | 1 | 6 |
| α-helix | 867-869 | 3 | |
| α-helix | 870-878 | 9 | |
| β-strand | 883-885 | 3 | 5 |
| α-helix | 892-894 | 3 | |
| α-helix | 896-901 | 6 | |
| β-strand | 905-910 | 6 | 7 |
| β-strand | 913-920 | 8 | 7 |
| α-helix | 924-938 | 15 | |
| α-helix | 948-956 | 9 | |
| β-strand | 960-965 | 6 | 5 |
| α-helix | 967-969 | 3 | |
| α-helix | 970-976 | 7 | |
| β-strand | 980-983 | 4 | 5 |
| α-helix | 984-986 | 3 | |
| β-strand | 987 | 1 | 6 |
| β-strand | 988 | 1 | 8 |
| β-strand | 991 | 1 | 8 |
| α-helix | 995 | 1 | |
| β-strand | 996-997 | 2 | 9 |
| β-strand | 998-1004 | 7 | 1 |
| β-strand | 1005 | 1 | 2 |
| α-helix | 1011-1016 | 6 | |
| α-helix | 1017-1022 | 6 | |
| α-helix | 1025-1034 | 10 | |
| β-strand | 1039-1040 | 2 | 1 |
| β-strand | 1042 | 1 | 3 |
| α-helix | 1043-1049 | 7 | |
| α-helix | 1053-1064 | 12 | |
| β-strand | 1066-1067 | 2 | 9 |
| α-helix | 1068-1069 | 2 | |
| α-helix | 1074-1090 | 17 | |
| α-helix | 1095-1105 | 11 | |
| β-strand | 1111 | 1 | 10 |
| β-strand | 1125 | 1 | 10 |
| β-strand | 1130-1133 | 4 | 11 |
| β-strand | 1144-1153 | 10 | 11 |
| β-strand | 1158-1163 | 6 | 11 |
| β-strand | 1167 | 1 | 12 |
| β-strand | 1170 | 1 | 12 |
| β-strand | 1174-1178 | 5 | 11 |
| α-helix | 1180-1182 | 3 | |
| β-strand | 1183-1186 | 4 | 11 |
| α-helix | 1194-1196 | 3 | |
| β-strand | 1200-1204 | 5 | 11 |
| α-helix | 1205 | 1 | |
| β-strand | 1210-1219 | 10 | 11 |
| α-helix | 1224 | 1 | |
| β-strand | 1225-1229 | 5 | 11 |
| β-strand | 1239-1241 | 3 | 11 |
| α-helix | 1243-1245 | 3 | |
| β-strand | 1246-1248 | 3 | 11 |
| α-helix | 1250-1253 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein,LINKER,SAGA-associated factor 29 | A | protein | 522 | Escherichia coli K-12, unidentified, Saccharomyces cerevisiae S288c | P0AEX9 (AlphaFold model), P25554 (AlphaFold model) |
| H3K4me2 peptide | P | protein | 4 | synthetic construct | P61830 (AlphaFold model) |
>3MP6_1 Maltose-binding periplasmic protein,LINKER,SAGA-associated factor 29 (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE ALAAAQTNAAAEFGSSYWTSEYNPNAPILVGSEVAYKPRRGSADGEWIQCEVLKVVADGT RFEVRDPEPDELGNSGKVYKCNRKELLLIPPGFPTKNYPPGTKVLARYPETTTFYPAIVI GTKRDGTCRLRFDGEEEVDKETEVTRRLVLPSPTALANLARK
>3MP6_2 H3K4me2 peptide (chains P) ARTK
Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. Bian, C., Xu, C., Ruan, J. et al. EMBO J (2011) 30:2829-2842. DOI 10.1038/emboj.2011.193 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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