Crystal structure of yeast Spt16 N-terminal Domain. Determined by X-ray diffraction at 1.94 Å resolution. Released 18 Dec 2007.
Explore 3BIP in 3D Show helices and sheets RCSB PDB PDBe
3BIP contains 41 α-helices and 42 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 | 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 | 71-76 | 6 | 1 |
| α-helix | 78-90 | 13 | |
| β-strand | 99-104 | 6 | 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 | 166-173 | 8 | |
| α-helix | 178-207 | 30 | |
| β-strand | 213 | 1 | 2 |
| α-helix | 214-222 | 9 | |
| α-helix | 223-226 | 4 | |
| 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 | 1 | 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 |
| β-strand | 412-421 | 10 | 4 |
| α-helix | 422-423 | 2 | |
| α-helix | 428-430 | 3 | |
| β-strand | 431-432 | 2 | 4 |
| α-helix | 440-442 | 3 | |
| β-strand | 444-445 | 2 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-21 | 14 | |
| α-helix | 22-24 | 3 | |
| β-strand | 31-36 | 6 | 5 |
| α-helix | 47-56 | 10 | |
| β-strand | 63-68 | 6 | 5 |
| β-strand | 71-77 | 7 | 5 |
| α-helix | 78-88 | 11 | |
| α-helix | 89-91 | 3 | |
| β-strand | 99-105 | 7 | 5 |
| α-helix | 110-127 | 18 | |
| β-strand | 130-133 | 4 | 5 |
| α-helix | 142-158 | 17 | |
| β-strand | 161-164 | 4 | 5 |
| α-helix | 166-172 | 7 | |
| α-helix | 178-207 | 30 | |
| β-strand | 213 | 1 | 6 |
| α-helix | 214-223 | 10 | |
| α-helix | 228-239 | 12 | |
| α-helix | 243 | 1 | |
| α-helix | 250-252 | 3 | |
| β-strand | 253-255 | 3 | 7 |
| β-strand | 260-262 | 3 | 8 |
| β-strand | 279 | 1 | 6 |
| β-strand | 284-290 | 7 | 8 |
| β-strand | 292-294 | 3 | 7 |
| β-strand | 297-298 | 2 | 7 |
| β-strand | 301-307 | 7 | 8 |
| α-helix | 311-326 | 16 | |
| α-helix | 327-331 | 5 | |
| α-helix | 338-352 | 15 | |
| α-helix | 354-359 | 6 | |
| β-strand | 360 | 1 | 8 |
| β-strand | 365-367 | 3 | 8 |
| β-strand | 378 | 1 | 8 |
| β-strand | 393-405 | 13 | 8 |
| β-strand | 408-421 | 14 | 8 |
| α-helix | 429-430 | 2 | |
| β-strand | 431-432 | 2 | 8 |
| α-helix | 440-443 | 4 | |
| β-strand | 444-445 | 2 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FACT complex subunit SPT16 | A, B | protein | 467 | Saccharomyces cerevisiae | P32558 (AlphaFold model) |
>3BIP_1 FACT complex subunit SPT16 (chains A, B) 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:
MolViewer shows 3BIP 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.