SETD2 in complex with a H3-variant super-substrate peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 29 Jan 2020.
Explore 6VDB in 3D Show helices and sheets RCSB PDB PDBe
6VDB contains 16 α-helices and 24 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 |
|---|---|---|---|
| α-helix | 1451-1455 | 5 | |
| α-helix | 1457-1465 | 9 | |
| α-helix | 1470-1472 | 3 | |
| β-strand | 1474-1475 | 2 | 1 |
| β-strand | 1480-1481 | 2 | 2 |
| α-helix | 1501-1505 | 5 | |
| α-helix | 1506-1510 | 5 | |
| α-helix | 1513-1514 | 2 | |
| β-strand | 1515 | 1 | 3 |
| α-helix | 1521-1524 | 4 | |
| β-strand | 1527 | 1 | 4 |
| α-helix | 1536-1538 | 3 | |
| β-strand | 1539 | 1 | 3 |
| β-strand | 1552-1556 | 5 | 5 |
| β-strand | 1562-1566 | 5 | 5 |
| β-strand | 1570 | 1 | 6 |
| β-strand | 1575-1578 | 4 | 4 |
| β-strand | 1582-1584 | 3 | 2 |
| α-helix | 1586-1599 | 14 | |
| β-strand | 1606-1610 | 5 | 2 |
| β-strand | 1613-1616 | 4 | 2 |
| β-strand | 1620-1621 | 2 | 1 |
| α-helix | 1623-1626 | 4 | |
| α-helix | 1627 | 1 | |
| β-strand | 1628-1629 | 2 | 7 |
| β-strand | 1635-1642 | 8 | 4 |
| β-strand | 1645-1652 | 8 | 4 |
| β-strand | 1656 | 1 | 6 |
| α-helix | 1660 | 1 | |
| β-strand | 1661 | 1 | 5 |
| α-helix | 1662 | 1 | |
| β-strand | 1663-1664 | 2 | 7 |
| β-strand | 1669-1670 | 2 | 8 |
| α-helix | 1675 | 1 | |
| β-strand | 1676-1677 | 2 | 9 |
| α-helix | 1678 | 1 | |
| β-strand | 1688-1689 | 2 | 9 |
| α-helix | 1697-1700 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-35 | 2 | 8 |
| β-strand | 36 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-lysine N-methyltransferase SETD2 | A | protein | 295 | Homo sapiens | Q9BYW2 (AlphaFold model) |
| Ala-pro-arg-phe-gly-gly-val-met-arg-pro-asn-arg | H | protein | 14 | synthetic construct |
>6VDB_1 Histone-lysine N-methyltransferase SETD2 (chains A) MHHHHHHSSGRENLYFQGETSVPPGSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLI EENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNG DYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEY ARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLV PSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRK
>6VDB_2 ALA-PRO-ARG-PHE-GLY-GLY-VAL-MET-ARG-PRO-ASN-ARG (chains H) APRFGGVMRPNRYR
| ID | Name | Formula | Copies |
|---|---|---|---|
| SCN | Thiocyanate ion | C N S | 1 |
| ZN | Zinc ion | Zn | 3 |
| SAH | S-adenosyl-L-homocysteine | C14 H20 N6 O5 S | 1 |
Water and common crystallization additives (UNX) are not listed.
Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate. Schuhmacher, M.K., Beldar, S., Khella, M.S. et al. Commun Biol (2020) 3:511-511. DOI 10.1038/s42003-020-01223-6 · PubMed
Other PDB entries of the same protein (UniProt Q9BYW2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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