N-Terminal domain of the yeast Not1. Determined by X-ray diffraction at 2.8 Å resolution. Released 21 Nov 2012.
Explore 4B8B in 3D Show helices and sheets RCSB PDB PDBe
4B8B contains 83 α-helices and 4 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 | 194-197 | 4 | |
| α-helix | 198-200 | 3 | |
| α-helix | 201-207 | 7 | |
| α-helix | 234-245 | 12 | |
| α-helix | 249-251 | 3 | |
| α-helix | 254-263 | 10 | |
| α-helix | 275-285 | 11 | |
| α-helix | 288-296 | 9 | |
| α-helix | 301-312 | 12 | |
| α-helix | 323-325 | 3 | |
| β-strand | 331 | 1 | 1 |
| α-helix | 343-345 | 3 | |
| β-strand | 346 | 1 | 1 |
| α-helix | 347-358 | 12 | |
| α-helix | 367-382 | 16 | |
| α-helix | 384-393 | 10 | |
| α-helix | 395-402 | 8 | |
| α-helix | 405-421 | 17 | |
| α-helix | 424-426 | 3 | |
| α-helix | 427-433 | 7 | |
| α-helix | 437-450 | 14 | |
| α-helix | 457-464 | 8 | |
| α-helix | 468-474 | 7 | |
| α-helix | 476 | 1 | |
| α-helix | 479-482 | 4 | |
| α-helix | 484-490 | 7 | |
| α-helix | 495-502 | 8 | |
| α-helix | 508-520 | 13 | |
| α-helix | 536-547 | 12 | |
| α-helix | 553-569 | 17 | |
| α-helix | 571-573 | 3 | |
| α-helix | 581-585 | 5 | |
| α-helix | 595-609 | 15 | |
| α-helix | 615-626 | 12 | |
| α-helix | 631-647 | 17 | |
| α-helix | 648-653 | 6 | |
| α-helix | 656-671 | 16 | |
| α-helix | 677-691 | 15 | |
| α-helix | 694 | 1 | |
| α-helix | 698-709 | 12 | |
| α-helix | 711-716 | 6 | |
| α-helix | 718-727 | 10 | |
| α-helix | 729-733 | 5 | |
| α-helix | 735-743 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 194-197 | 4 | |
| α-helix | 200-206 | 7 | |
| α-helix | 235-245 | 11 | |
| α-helix | 249-251 | 3 | |
| α-helix | 254-263 | 10 | |
| α-helix | 275-285 | 11 | |
| α-helix | 288-296 | 9 | |
| α-helix | 301-312 | 12 | |
| α-helix | 316-318 | 3 | |
| β-strand | 331 | 1 | 2 |
| α-helix | 343-345 | 3 | |
| β-strand | 346 | 1 | 2 |
| α-helix | 347-358 | 12 | |
| α-helix | 360-362 | 3 | |
| α-helix | 367-382 | 16 | |
| α-helix | 384-393 | 10 | |
| α-helix | 395-402 | 8 | |
| α-helix | 405-421 | 17 | |
| α-helix | 424-426 | 3 | |
| α-helix | 427-432 | 6 | |
| α-helix | 437-450 | 14 | |
| α-helix | 457-464 | 8 | |
| α-helix | 468-474 | 7 | |
| α-helix | 476 | 1 | |
| α-helix | 480-490 | 11 | |
| α-helix | 495-502 | 8 | |
| α-helix | 508-520 | 13 | |
| α-helix | 536-548 | 13 | |
| α-helix | 553-569 | 17 | |
| α-helix | 571-573 | 3 | |
| α-helix | 581-585 | 5 | |
| α-helix | 595-609 | 15 | |
| α-helix | 615-625 | 11 | |
| α-helix | 631-647 | 17 | |
| α-helix | 648-653 | 6 | |
| α-helix | 656-671 | 16 | |
| α-helix | 677-691 | 15 | |
| α-helix | 694 | 1 | |
| α-helix | 698-709 | 12 | |
| α-helix | 711-716 | 6 | |
| α-helix | 718-727 | 10 | |
| α-helix | 729-733 | 5 | |
| α-helix | 735-742 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| General negative regulator of transcription subunit 1 | A, B | protein | 603 | SACCHAROMYCES CEREVISIAE S288C | P25655 (AlphaFold model) |
>4B8B_1 GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1 (chains A, B) RSSQINDFKTIKMNHTNYLRNFFLQTTPETLESNLRDLLHSLEGESLNDLLALLLSEILS PGSQNLQNDPTRSWLTPPMVLDATNRGNVIARSISSLQANQINWNRVFNLMSTKYFLSAP LMPTTASLSCLFAALHDGPVIDEFFSCDWKVIFKLDLAIQLHKWSVQNGCFDLLNAEGTR KVSETIPNTKQSLLYLLSIASLNLELFLQREELSDGPMLAYFQECFFEDFNYAPEYLILA LVKEMKRFVLLIENRTVIDEILITLLIQVHNKSPSSFKDVISTITDDSKIVDAAKIIINS DDAPIANFLKSLLDTGRLDTVINKLPFNEAFKILPCARQIGWEGFDTFLKTKVSPSNVDV VLESLEVQTKMTDTNTPFRSLKTFDLFAFHSLIEVLNKCPLDVLQLQRFESLEFSLLIAF PRLINFGFGHDEAILANGDIAGINNDIEKEMQNYLQKMYSGELAIKDVIELLRRLRDSDL PRDQEVFTCITHAVIAESTFFQDYPLDALATTSVLFGSMILFQLLRGFVLDVAFRIIMRF AKEPPESKMFKFAVQAIYAFRIRLAEYPQYCKDLLRDVPALKSQAQVYQSIVEAATLANA PKE
| ID | Name | Formula | Copies |
|---|---|---|---|
| AU | Gold ion | Au | 29 |
Architecture of the Nuclease Module of the Yeast Ccr4-not Complex: The not1-Caf1-Ccr4 Interaction. Basquin, J., Roudko, V.V., Rode, M. et al. Mol Cell (2012) 48:207. DOI 10.1016/J.MOLCEL.2012.08.014 · PubMed
Other PDB entries of the same protein (UniProt P25655 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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