Structure of fission yeast Mis16 bound to histone H4. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Aug 2019.
Explore 6S1R in 3D Show helices and sheets RCSB PDB PDBe
6S1R contains 10 α-helices and 29 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 | 13-40 | 28 | |
| β-strand | 41-48 | 8 | 1 |
| β-strand | 56-64 | 9 | 2 |
| β-strand | 70-77 | 8 | 2 |
| α-helix | 86 | 1 | |
| β-strand | 87-97 | 11 | 2 |
| β-strand | 122-130 | 9 | 2 |
| β-strand | 136-140 | 5 | 3 |
| β-strand | 143-150 | 8 | 3 |
| α-helix | 152-154 | 3 | |
| β-strand | 156-160 | 5 | 3 |
| α-helix | 171-174 | 4 | |
| β-strand | 176-178 | 3 | 3 |
| β-strand | 185-190 | 6 | 4 |
| β-strand | 197-202 | 6 | 4 |
| β-strand | 207-211 | 5 | 4 |
| α-helix | 214-216 | 3 | |
| α-helix | 222 | 1 | |
| β-strand | 223-225 | 3 | 3 |
| β-strand | 229-231 | 3 | 4 |
| β-strand | 238-243 | 6 | 5 |
| β-strand | 250-255 | 6 | 5 |
| β-strand | 260-264 | 5 | 5 |
| β-strand | 275-277 | 3 | 5 |
| β-strand | 284-289 | 6 | 6 |
| β-strand | 296-301 | 6 | 6 |
| β-strand | 306-310 | 5 | 6 |
| β-strand | 317-321 | 5 | 6 |
| β-strand | 328-333 | 6 | 7 |
| β-strand | 340-345 | 6 | 7 |
| β-strand | 350-354 | 5 | 7 |
| α-helix | 355-357 | 3 | |
| α-helix | 364-369 | 6 | |
| β-strand | 374-378 | 5 | 7 |
| β-strand | 385-390 | 6 | 1 |
| β-strand | 398-402 | 5 | 1 |
| β-strand | 406-412 | 7 | 1 |
| α-helix | 414-417 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 32-40 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase type B subunit 2 | A | protein | 430 | Schizosaccharomyces pombe | O94244 (AlphaFold model) |
| Histone H4 | B | protein | 31 | Schizosaccharomyces pombe | P09322 (AlphaFold model) |
>6S1R_1 Histone acetyltransferase type B subunit 2 (chains A) GSEEVVQDAPLENNELNAEIDLQKTIQEEYKLWKQNVPFLYDLVITHALEWPSLTIQWLP DKKTIPGTDYSIQRLILGTHTSGNDQNYLQIASVQLPNFDEDTTEFTPSTIRRAQATGSY TIEISQKIPHDGDVNRARYMPQKPEIIATMGEGGNAYIFDTTCHDALTTGEALPQAVLKG HTAEGFGLCWNPNLPGNLATGAEDQVICLWDVQTQSFTSSETKVISPIAKYHRHTDIVND VQFHPQHEALLASVSDDCTLQIHDTRLNPEEEAPKVIQAHSKAINAVAINPFNDYLLATA SADKTVALWDLRNPYQRLHTLEGHEDEVYGLEWSPHDEPILASSSTDRRVCIWDLEKIGE EQTPEDAEDGSPELLFMHGGHTNRISEFSWCPNERWVVGSLADDNILQIWSPSRVIWGRD HVQVSPRDLE
>6S1R_2 Histone H4 (chains B) GGAKRHRKILRDNIQGITKPAIRRLARRGGV
Subunit interactions and arrangements in the fission yeast Mis16-Mis18-Mis19 complex. Korntner-Vetter, M., Lefevre, S., Hu, X.W. et al. Life Sci Alliance (2019) 2. DOI 10.26508/lsa.201900408 · PubMed
Other PDB entries of the same protein (UniProt O94244 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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