Cocrystal structure of human SMYD3 with inhibitor Sinefungin bound. Determined by X-ray diffraction at 1.85 Å resolution. Released 18 May 2011.
Explore 3RU0 in 3D Show helices and sheets RCSB PDB PDBe
3RU0 contains 48 α-helices and 35 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 | 6-10 | 5 | 1 |
| β-strand | 16-20 | 5 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-33 | 5 | 3 |
| β-strand | 37-40 | 4 | 4 |
| β-strand | 48 | 1 | 5 |
| β-strand | 55 | 1 | 5 |
| β-strand | 60-61 | 2 | 6 |
| α-helix | 62 | 1 | |
| β-strand | 69-70 | 2 | 6 |
| α-helix | 73-83 | 11 | |
| α-helix | 87-93 | 7 | |
| α-helix | 100-111 | 12 | |
| α-helix | 117-118 | 2 | |
| α-helix | 119-121 | 3 | |
| α-helix | 126-128 | 3 | |
| α-helix | 133-135 | 3 | |
| α-helix | 138-154 | 17 | |
| α-helix | 162-164 | 3 | |
| α-helix | 171-181 | 11 | |
| β-strand | 183-186 | 4 | 4 |
| β-strand | 192-197 | 6 | 4 |
| α-helix | 201-203 | 3 | |
| α-helix | 204 | 1 | |
| β-strand | 205-206 | 2 | 7 |
| β-strand | 212-217 | 6 | 3 |
| β-strand | 220-225 | 6 | 3 |
| β-strand | 229 | 1 | 2 |
| α-helix | 233 | 1 | |
| β-strand | 234-235 | 2 | 1 |
| β-strand | 236-237 | 2 | 7 |
| α-helix | 246-257 | 12 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-275 | 4 | |
| α-helix | 280-298 | 19 | |
| α-helix | 302-316 | 15 | |
| α-helix | 325-340 | 16 | |
| α-helix | 344-361 | 18 | |
| α-helix | 367-382 | 16 | |
| α-helix | 386-403 | 18 | |
| α-helix | 409-427 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 8 |
| β-strand | 16-20 | 5 | 8 |
| β-strand | 24 | 1 | 9 |
| β-strand | 29-33 | 5 | 10 |
| β-strand | 37-40 | 4 | 11 |
| α-helix | 42-44 | 3 | |
| β-strand | 45 | 1 | 12 |
| β-strand | 48 | 1 | 12 |
| β-strand | 55 | 1 | 12 |
| β-strand | 60-61 | 2 | 13 |
| β-strand | 69-70 | 2 | 13 |
| α-helix | 73-83 | 11 | |
| α-helix | 87-93 | 7 | |
| α-helix | 100-111 | 12 | |
| α-helix | 117-118 | 2 | |
| α-helix | 119-121 | 3 | |
| α-helix | 133-135 | 3 | |
| α-helix | 138-154 | 17 | |
| α-helix | 162-164 | 3 | |
| α-helix | 171-181 | 11 | |
| β-strand | 183-186 | 4 | 11 |
| β-strand | 192-197 | 6 | 11 |
| α-helix | 201-203 | 3 | |
| α-helix | 204 | 1 | |
| β-strand | 205-206 | 2 | 14 |
| β-strand | 212-217 | 6 | 10 |
| β-strand | 220-225 | 6 | 10 |
| β-strand | 229 | 1 | 9 |
| α-helix | 233 | 1 | |
| β-strand | 234-235 | 2 | 8 |
| β-strand | 236-237 | 2 | 14 |
| α-helix | 246-257 | 12 | |
| α-helix | 264-268 | 5 | |
| α-helix | 272-275 | 4 | |
| α-helix | 280-298 | 19 | |
| α-helix | 302-315 | 14 | |
| α-helix | 325-341 | 17 | |
| α-helix | 344-353 | 10 | |
| α-helix | 355-361 | 7 | |
| α-helix | 367-382 | 16 | |
| α-helix | 386-403 | 18 | |
| α-helix | 409-421 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SET and MYND domain-containing protein 3 | A, B | protein | 438 | Homo sapiens | Q9H7B4 (AlphaFold model) |
>3RU0_1 SET and MYND domain-containing protein 3 (chains A, B) MALEPLKVEKFATANRGNGLRAVTPLRPGELLFRSDPLAYTVCKGSRGVVCDRCLLGKEK LMRCSQCRVAKYCSAKCQKKAWPDHKRECKCLKSCKPRYPPDSVRLLGRVVFKLMDGAPS ESEKLYSFYDLESNINKLTEDKKEGLRQLVMTFQHFMREEIQDASQLPPAFDLFEAFAKV ICNSFTICNAEMQEVGVGLYPSISLLNHSCDPNCSIVFNGPHLLLRAVRDIEVGEELTIC YLDMLMTSEERRKQLRDQYCFECDCFRCQTQDKDADMLTGDEQVWKEVQESLKKIEELKA HWKWEQVLAMCQAIISSNSERLPDINIYQLKVLDCAMDACINLGLLEEALFYGTRTMEPY RIFFPGSHPVRGVQVMKVGKLQLHQGMFPQAMKNLRLAFDIMRVTHGREHSLIEDLILLL EECDANIRASEGHHHHHH
Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3. Foreman, K.W., Brown, M., Park, F. et al. PLoS One (2011) 6:e22290-e22290. DOI 10.1371/journal.pone.0022290 · PubMed
Other PDB entries of the same protein (UniProt Q9H7B4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3RU0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.