Structural Basis for the Hierarchical Assembly of the Core of PRC1.1. Determined by X-ray diffraction at 2.55 Å resolution. Released 14 Sept 2016.
Explore 5JH5 in 3D Show helices and sheets RCSB PDB PDBe
5JH5 contains 34 α-helices and 30 β-strands across 4 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 | 1067-1074 | 8 | |
| α-helix | 1079-1086 | 8 | |
| α-helix | 1092-1095 | 4 | |
| α-helix | 1099-1102 | 4 | |
| β-strand | 1104-1106 | 3 | 1 |
| α-helix | 1115-1124 | 10 | |
| β-strand | 1128-1130 | 3 | 1 |
| α-helix | 1138-1147 | 10 | |
| β-strand | 1153-1155 | 3 | 1 |
| β-strand | 1160 | 1 | 2 |
| α-helix | 1161-1164 | 4 | |
| α-helix | 1165-1168 | 4 | |
| β-strand | 1177-1179 | 3 | 1 |
| β-strand | 1184 | 1 | 2 |
| β-strand | 1187 | 1 | 3 |
| α-helix | 1188-1195 | 8 | |
| β-strand | 1217-1219 | 3 | 1 |
| β-strand | 1224 | 1 | 3 |
| α-helix | 1227-1236 | 10 | |
| β-strand | 1242-1244 | 3 | 1 |
| α-helix | 1253-1259 | 7 | |
| α-helix | 1265-1269 | 5 | |
| β-strand | 1272-1274 | 3 | 1 |
| α-helix | 1284-1289 | 6 | |
| β-strand | 1297-1299 | 3 | 1 |
| α-helix | 1308-1318 | 11 | |
| β-strand | 1324-1325 | 2 | 1 |
| β-strand | 1331-1334 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 4 |
| β-strand | 13-17 | 5 | 4 |
| α-helix | 18-21 | 4 | |
| α-helix | 25-33 | 9 | |
| β-strand | 45-46 | 2 | 4 |
| α-helix | 52-64 | 13 | |
| α-helix | 68-72 | 5 | |
| α-helix | 87-92 | 6 | |
| α-helix | 97-110 | 14 | |
| α-helix | 113-125 | 13 | |
| α-helix | 132-139 | 8 | |
| α-helix | 147-156 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 163-165 | 3 | |
| β-strand | 168-175 | 8 | 5 |
| β-strand | 190-195 | 6 | 5 |
| β-strand | 199 | 1 | 6 |
| α-helix | 200-211 | 12 | |
| α-helix | 215-217 | 3 | |
| β-strand | 218-222 | 5 | 5 |
| β-strand | 225-226 | 2 | 5 |
| α-helix | 227-228 | 2 | |
| β-strand | 232 | 1 | 6 |
| α-helix | 233-240 | 8 | |
| α-helix | 244-245 | 2 | |
| α-helix | 247 | 1 | |
| β-strand | 248-254 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1596-1601 | 6 | 5 |
| β-strand | 1608-1611 | 4 | 7 |
| β-strand | 1620-1624 | 5 | 7 |
| α-helix | 1625-1632 | 8 | |
| α-helix | 1636-1642 | 7 | |
| β-strand | 1648-1652 | 5 | 7 |
| α-helix | 1653-1661 | 9 | |
| β-strand | 1686-1691 | 6 | 7 |
| α-helix | 1694-1699 | 6 | |
| β-strand | 1703-1707 | 5 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine-specific demethylase 2B | A | protein | 281 | Homo sapiens | Q8NHM5 (AlphaFold model) |
| S-phase kinase-associated protein 1 | B | protein | 162 | Homo sapiens | P63208 (AlphaFold model) |
| Polycomb group RING finger protein 1 | C | protein | 109 | Homo sapiens | Q9BSM1 (AlphaFold model) |
| BCL-6 corepressor-like protein 1 | D | protein | 122 | Homo sapiens | Q5H9F3 (AlphaFold model) |
>5JH5_1 Lysine-specific demethylase 2B (chains A) GTRDGAAHVMHREVWMAVFSYLSHQDLCVCMRVCRTWNRWCCDKRLWTRIDLNHCKSITP LMLSGIIRRQPVSLDLSWTNISKKQLSWLINRLPGLRDLVLSGCSWIAVSALCSSSCPLL RTLDVQWVEGLKDAQMRDLLSPPTDNRPGQMDNRSKLRNIVELRLAGLDITDASLRLIIR HMPLLSKLHLSYCNHVTDQSINLLTAVGTTTRDSLTEINLSDCNKVTDQCLSFFKRCGNI CHIDLRYCKQVTKEGCEQFIAEMSVSVQFGQVEEKLLQKLS
>5JH5_2 S-phase kinase-associated protein 1 (chains B) PSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQW CTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTCK TVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
>5JH5_3 Polycomb group RING finger protein 1 (chains C) GTRLPFSSFDHSKAHYYRYDEQLNLCLERLSSGKDKNKSVLQNKYVRCSVRAEVRHLRRV LCHRLMLNPQHVQLLFDNEVLPDHMTMKQIWLSRWFGKPSPLLLQYSVK
>5JH5_4 BCL-6 corepressor-like protein 1 (chains D) METRDDFMFELSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEIT TMPKAEFYRQVASSQLLTPAERPGGLDDRSPPGSSETVELVRYEPDLLRLLGSEVEFQSC NS
KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1. Wong, S.J., Gearhart, M.D., Taylor, A.B. et al. Structure (2016) 24:1795-1801. DOI 10.1016/j.str.2016.07.011 · PubMed
Other PDB entries of the same protein (UniProt Q8NHM5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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