Crystal structure of t131 N-terminal TPR array. Determined by X-ray diffraction at 3.15 Å resolution. Released 24 Jun 2015.
Explore 5AIO in 3D Show helices and sheets RCSB PDB PDBe
5AIO contains 31 α-helices and 0 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 | 133-141 | 9 | |
| α-helix | 146-150 | 5 | |
| α-helix | 151-157 | 7 | |
| α-helix | 162-175 | 14 | |
| α-helix | 178-189 | 12 | |
| α-helix | 196-208 | 13 | |
| α-helix | 212-225 | 14 | |
| α-helix | 230-243 | 14 | |
| α-helix | 246-259 | 14 | |
| α-helix | 264-276 | 13 | |
| α-helix | 280-314 | 35 | |
| α-helix | 344-349 | 6 | |
| α-helix | 352-354 | 3 | |
| α-helix | 357-370 | 14 | |
| α-helix | 374-387 | 14 | |
| α-helix | 388-390 | 3 | |
| α-helix | 396-399 | 4 | |
| α-helix | 408-412 | 5 | |
| α-helix | 414-418 | 5 | |
| α-helix | 432-443 | 12 | |
| α-helix | 448-455 | 8 | |
| α-helix | 456-458 | 3 | |
| α-helix | 463-466 | 4 | |
| α-helix | 467-479 | 13 | |
| α-helix | 483-490 | 8 | |
| α-helix | 491-495 | 5 | |
| α-helix | 497-499 | 3 | |
| α-helix | 502-514 | 13 | |
| α-helix | 518-530 | 13 | |
| α-helix | 536-548 | 13 | |
| α-helix | 552-563 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription factor tau 131 kda subunit | A | protein | 448 | SACCHAROMYCES CEREVISIAE | P33339 (AlphaFold model) |
>5AIO_1 TRANSCRIPTION FACTOR TAU 131 KDA SUBUNIT (chains A) GAMAVLDPEVAQLLSQANEAFVRNDLQVAERLFNEVIKKDARNFAAYETLGDIYQLQGRL NDCCNSWFLAAHLNASDWEFWKIVAILSADLDHVRQAIYCFSRVISLNPMEWESIYRRSM LYKKTGQLARALDGFQRLYMYNPYDANILRELAILYVDYDRIEDSIELYMKVFNANVERR EAILAALENALDSSDEESAAEGEDADEKEPLEQDEDRQMFPDINWKKIDAKYKCIPFDWS SLNILAELFLKLAVSEVDGIKTIKKCARWIQRRESQTFWDHVPDDSEFDNRRFKNSTFDS LLAAEKEKSYNIPIDIRVRLGLLRLNTDNLVEALNHFQCLYDETFSDVADLYFEAATALT RAEKYKEAIDFFTPLLSLEEWRTTDVFKPLARCYKEIESYETAKEFYELAIKSEPDDLDI RVSLAEVYYRLNDPETFKHMLVDVVEMR
Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. Male, G., von Appen, A., Glatt, S. et al. Nat Commun (2015) 6:7387-7387. DOI 10.1038/ncomms8387 · PubMed
Other PDB entries of the same protein (UniProt P33339 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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