Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-15. Determined by X-ray diffraction at 1.55 Å resolution. Released 2 Jan 2013.
Explore 4GNF in 3D Show helices and sheets RCSB PDB PDBe
4GNF contains 4 α-helices and 11 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 |
|---|---|---|---|
| β-strand | 1332-1335 | 4 | 1 |
| β-strand | 1344-1345 | 2 | 1 |
| α-helix | 1348-1350 | 3 | |
| α-helix | 1355-1357 | 3 | |
| α-helix | 1363-1365 | 3 | |
| β-strand | 1366 | 1 | 2 |
| β-strand | 1373 | 1 | 2 |
| α-helix | 1374 | 1 | |
| β-strand | 1376-1377 | 2 | 3 |
| β-strand | 1384-1385 | 2 | 3 |
| β-strand | 1395-1396 | 2 | 4 |
| β-strand | 1403-1404 | 2 | 4 |
| β-strand | 1409 | 1 | 5 |
| β-strand | 1412 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-lysine N-methyltransferase NSD3 | A | protein | 107 | Homo sapiens | Q9BZ95 (AlphaFold model) |
| Histone H3.3 | C | protein | 15 | Homo sapiens | P84243 (AlphaFold model) |
>4GNF_1 Histone-lysine N-methyltransferase NSD3 (chains A) SNARKIKTEPKQMHEDYCFQCGDGGELVMCDKKDCPKAYHLLCLNLTQPPYGKWECPWHQ CDECSSAAVSFCEFCPHSFCKDHEKGALVPSALEGRLCCSEHDPMAP
>4GNF_2 Histone H3.3 (chains C) ARTKQTARKSTGGKA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
The methyltransferase NSD3 has chromatin-binding motifs, PHD5-C5HCH, that are distinct from other NSD (nuclear receptor SET domain) family members in their histone H3 recognition. He, C., Li, F., Zhang, J. et al. J Biol Chem (2013) 288:4692-4703. DOI 10.1074/jbc.M112.426148 · PubMed
Other PDB entries of the same protein (UniProt Q9BZ95 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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