free KDM6B structure. Determined by X-ray diffraction at 2.99 Å resolution. Released 8 Aug 2012.
Explore 4EZ4 in 3D Show helices and sheets RCSB PDB PDBe
4EZ4 contains 49 α-helices and 46 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 | 1162-1164 | 3 | |
| α-helix | 1175-1177 | 3 | |
| α-helix | 1178-1181 | 4 | |
| α-helix | 1183-1186 | 4 | |
| β-strand | 1187-1189 | 3 | 1 |
| α-helix | 1193-1197 | 5 | |
| α-helix | 1199-1206 | 8 | |
| β-strand | 1212-1216 | 5 | 1 |
| α-helix | 1218-1222 | 5 | |
| α-helix | 1226-1229 | 4 | |
| α-helix | 1231-1237 | 7 | |
| β-strand | 1242-1248 | 7 | 1 |
| β-strand | 1257 | 1 | 2 |
| β-strand | 1264 | 1 | 2 |
| β-strand | 1267 | 1 | 3 |
| β-strand | 1271-1276 | 6 | 1 |
| α-helix | 1277-1294 | 18 | |
| β-strand | 1326-1333 | 8 | 1 |
| α-helix | 1341-1344 | 4 | |
| α-helix | 1352-1354 | 3 | |
| α-helix | 1362-1365 | 4 | |
| β-strand | 1377-1381 | 5 | 1 |
| β-strand | 1386-1390 | 5 | 4 |
| α-helix | 1393-1395 | 3 | |
| β-strand | 1397-1405 | 9 | 1 |
| β-strand | 1408-1413 | 6 | 4 |
| α-helix | 1415-1417 | 3 | |
| α-helix | 1418-1428 | 11 | |
| β-strand | 1437 | 1 | 3 |
| α-helix | 1441-1446 | 6 | |
| β-strand | 1452-1456 | 5 | 4 |
| β-strand | 1461-1464 | 4 | 1 |
| α-helix | 1465 | 1 | |
| β-strand | 1469-1474 | 6 | 4 |
| β-strand | 1478-1485 | 8 | 1 |
| α-helix | 1490-1506 | 17 | |
| α-helix | 1514-1524 | 11 | |
| α-helix | 1530-1555 | 26 | |
| β-strand | 1561-1563 | 3 | 5 |
| α-helix | 1570-1572 | 3 | |
| β-strand | 1573-1574 | 2 | 6 |
| β-strand | 1581-1582 | 2 | 6 |
| β-strand | 1586-1590 | 5 | 5 |
| β-strand | 1598-1601 | 4 | 5 |
| α-helix | 1603-1609 | 7 | |
| β-strand | 1617-1620 | 4 | 5 |
| α-helix | 1624-1632 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1162-1164 | 3 | |
| α-helix | 1167-1169 | 3 | |
| α-helix | 1178-1181 | 4 | |
| α-helix | 1183-1186 | 4 | |
| β-strand | 1187-1189 | 3 | 7 |
| α-helix | 1193-1197 | 5 | |
| α-helix | 1199-1206 | 8 | |
| β-strand | 1212-1216 | 5 | 7 |
| α-helix | 1218-1222 | 5 | |
| α-helix | 1231-1237 | 7 | |
| β-strand | 1242-1249 | 8 | 7 |
| β-strand | 1257 | 1 | 8 |
| β-strand | 1264 | 1 | 8 |
| β-strand | 1267 | 1 | 9 |
| β-strand | 1271-1276 | 6 | 7 |
| α-helix | 1277-1293 | 17 | |
| β-strand | 1325-1333 | 9 | 7 |
| α-helix | 1341-1346 | 6 | |
| α-helix | 1352-1354 | 3 | |
| α-helix | 1362-1364 | 3 | |
| β-strand | 1377-1381 | 5 | 7 |
| β-strand | 1386-1390 | 5 | 10 |
| α-helix | 1393-1395 | 3 | |
| β-strand | 1397-1405 | 9 | 7 |
| β-strand | 1408-1413 | 6 | 10 |
| α-helix | 1415-1417 | 3 | |
| α-helix | 1418-1428 | 11 | |
| β-strand | 1437 | 1 | 9 |
| α-helix | 1441-1446 | 6 | |
| β-strand | 1452-1456 | 5 | 10 |
| α-helix | 1460 | 1 | |
| β-strand | 1461-1464 | 4 | 7 |
| α-helix | 1465 | 1 | |
| β-strand | 1469-1474 | 6 | 10 |
| β-strand | 1478-1485 | 8 | 7 |
| α-helix | 1490-1506 | 17 | |
| α-helix | 1508-1510 | 3 | |
| α-helix | 1514-1524 | 11 | |
| α-helix | 1530-1555 | 26 | |
| β-strand | 1561-1563 | 3 | 11 |
| α-helix | 1570-1572 | 3 | |
| β-strand | 1573-1574 | 2 | 12 |
| β-strand | 1581-1582 | 2 | 12 |
| β-strand | 1586-1589 | 4 | 11 |
| β-strand | 1599-1601 | 3 | 11 |
| α-helix | 1603-1609 | 7 | |
| β-strand | 1617-1620 | 4 | 11 |
| α-helix | 1624-1632 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine-specific demethylase 6B | A, B | protein | 486 | Mus musculus | Q5NCY0 (AlphaFold model) |
>4EZ4_1 Lysine-specific demethylase 6B (chains A, B) ESYLSPAQSVKPKINTEEKLPREKLNPPTPSIYLESKRDAFSPVLLQFCTDPRNPITVIR GLAGSLRLNLGLFSTKTLVEASGEHTVEVRTQVQQPSDENWDLTGTRQIWPCESSRSHTT IAKYAQYQASSFQESLQEELEVLFQGPTKAARKSAPATGGGSSGSHHIIKFGTNIDLSDA KRWKPQLQELLKLPAFMRVTSTGNMLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFC SVNINIGPGDCEWFAVHEHYWETISAFCDRHGVDYLTGSWWPILDDLYASNIPVYRFVQR PGDLVWINAGTVHWVQATGWCNNIAWNVGPLTAYQYQLALERYEWNEVKNVKSIVPMIHV SWNVARTVKISDPDLFKMIKFCLLQSMKHCQVQRESLVRAGKKIAYQGRVKDEPAYYCNE CDVEVFNILFVTSENGSRNTYLVHCEGCARRRSAGLQGVVVLEQYRTEELAQAYDAFTLA PASTSR
A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. Kruidenier, L., Chung, C.W., Cheng, Z. et al. Nature (2012) 488:404-408. DOI 10.1038/nature11262 · PubMed
Other PDB entries of the same protein (UniProt Q5NCY0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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