Crystal structure of yeast Spt16 N-terminal Domain. Determined by X-ray diffraction at 1.73 Å resolution. Released 18 Dec 2007.
Explore 3BIQ in 3D Show helices and sheets RCSB PDB PDBe
3BIQ contains 24 α-helices and 21 β-strands across 1 chain. 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 | 8-21 | 14 | |
| α-helix | 22-24 | 3 | |
| β-strand | 31-36 | 6 | 1 |
| α-helix | 47-56 | 10 | |
| β-strand | 63-68 | 6 | 1 |
| β-strand | 71-77 | 7 | 1 |
| α-helix | 78-88 | 11 | |
| α-helix | 89-91 | 3 | |
| β-strand | 99-105 | 7 | 1 |
| α-helix | 110-127 | 18 | |
| β-strand | 130-133 | 4 | 1 |
| α-helix | 142-158 | 17 | |
| β-strand | 161-164 | 4 | 1 |
| α-helix | 166-172 | 7 | |
| α-helix | 176-177 | 2 | |
| α-helix | 178-207 | 30 | |
| β-strand | 213 | 1 | 2 |
| α-helix | 214-223 | 10 | |
| α-helix | 224-226 | 3 | |
| α-helix | 228-239 | 12 | |
| α-helix | 243 | 1 | |
| α-helix | 250-252 | 3 | |
| β-strand | 253-255 | 3 | 3 |
| β-strand | 260-262 | 3 | 4 |
| β-strand | 279 | 1 | 2 |
| α-helix | 280 | 1 | |
| β-strand | 284-290 | 7 | 4 |
| β-strand | 292-294 | 3 | 3 |
| β-strand | 297-298 | 2 | 3 |
| β-strand | 301-307 | 7 | 4 |
| α-helix | 311-326 | 16 | |
| α-helix | 327-331 | 5 | |
| α-helix | 338-352 | 15 | |
| α-helix | 354-359 | 6 | |
| β-strand | 360 | 1 | 4 |
| β-strand | 365-367 | 3 | 4 |
| α-helix | 375-377 | 3 | |
| β-strand | 378 | 1 | 4 |
| β-strand | 393-403 | 11 | 4 |
| α-helix | 404-405 | 2 | |
| β-strand | 412-421 | 10 | 4 |
| α-helix | 429-430 | 2 | |
| β-strand | 431-432 | 2 | 4 |
| α-helix | 440-443 | 4 | |
| β-strand | 444-445 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FACT complex subunit SPT16 | A | protein | 467 | Saccharomyces cerevisiae | P32558 (AlphaFold model) |
>3BIQ_1 FACT complex subunit SPT16 (chains A) GHMEELNIDFDVFKKRIELLYSKYNEFEGSPNSLLFVLGSSNAENPYQKTTILHNWLLSY EFPATLIALVPGKVIIITSSAKAKHLQKAIDLFKDPESKITLELWQRNNKEPELNKKLFD DVIALINSAGKTVGIPEKDSYQGKFMTEWNPVWEAAVKENEFNVIDISLGLSKVWEVKDV NEQAFLSVSSKGSDKFMDLLSNEMVRAVDEELKITNAKLSDKIENKIDDVKFLKQLSPDL SALCPPNYKFNFDLLDWTYSPIIQSGKKFDLRVSARSTNDQLYGNGCILASCGIRYNNYC SNITRTFLIDPSEEMANNYDFLLTLQKEIVTNILKPGRTPKEVYESVIEYIEKTKPELVP NFTKNIGSLIGLEFRDSNFILNVKNDYRKIQRGDCFNISFGFNNLKDSQSANNYALQLAD TVQIPLDETEPPRFLTNYTKAKSQISFYFNNEEEDNNKKKSSPATKV
Structural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunits. VanDemark, A.P., Xin, H., McCullough, L. et al. J Biol Chem (2008) 283:5058-5068. DOI 10.1074/jbc.M708682200 · PubMed
Other PDB entries of the same protein (UniProt P32558 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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