Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction. Determined by X-ray diffraction at 3.3 Å resolution. Released 28 Apr 2010.
Explore 3AAD in 3D Show helices and sheets RCSB PDB PDBe
3AAD contains 25 α-helices and 24 β-strands across 3 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 | 1381-1396 | 16 | |
| α-helix | 1403-1405 | 3 | |
| α-helix | 1417-1420 | 4 | |
| α-helix | 1427-1435 | 9 | |
| α-helix | 1442-1459 | 18 | |
| α-helix | 1465-1470 | 6 | |
| α-helix | 1472-1475 | 4 | |
| α-helix | 1481-1483 | 3 | |
| α-helix | 1485-1493 | 9 | |
| α-helix | 1502-1513 | 12 | |
| α-helix | 1514-1518 | 5 | |
| α-helix | 1519-1521 | 3 | |
| α-helix | 1526-1528 | 3 | |
| α-helix | 1531-1533 | 3 | |
| α-helix | 1540-1543 | 4 | |
| α-helix | 1550-1558 | 9 | |
| α-helix | 1565-1583 | 19 | |
| α-helix | 1588-1627 | 40 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-8 | 5 | 1 |
| β-strand | 11 | 1 | 1 |
| β-strand | 16-17 | 2 | 2 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 1 |
| β-strand | 40-45 | 6 | 2 |
| β-strand | 55-60 | 6 | 2 |
| β-strand | 68-76 | 9 | 1 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| β-strand | 92-101 | 10 | 2 |
| β-strand | 104-117 | 14 | 2 |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 2 |
| β-strand | 145-148 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 3 |
| β-strand | 11 | 1 | 4 |
| β-strand | 16-17 | 2 | 5 |
| α-helix | 21 | 1 | |
| β-strand | 22-24 | 3 | 4 |
| β-strand | 27-30 | 4 | 3 |
| β-strand | 39-44 | 6 | 5 |
| β-strand | 55-60 | 6 | 5 |
| β-strand | 68-71 | 4 | 3 |
| β-strand | 74-76 | 3 | 4 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| β-strand | 91-101 | 11 | 5 |
| β-strand | 104-117 | 14 | 5 |
| β-strand | 135-139 | 5 | 5 |
| β-strand | 145-147 | 3 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription initiation factor TFIID subunit 1 | A | protein | 292 | Homo sapiens | P21675 (AlphaFold model) |
| Histone chaperone ASF1A | B, D | protein | 158 | Homo sapiens | Q9Y294 (AlphaFold model) |
>3AAD_1 Transcription initiation factor TFIID subunit 1 (chains A) GSHMVLKFPKQQLPPKKKRRVGTTVHCDYLNRPHKSIHRRRTDPMVTLSSILESIINDMR DLPNTYPFHTPVNAKVVKDYYKIITRPMDLQTLRENVRKRLYPSREEFREHLELIVKNSA TYNGPKHSLTQISQSMLDLCDEKLKEKEDKLARLEKAINPLLDDDDQVAFSFILDNIVTQ KMMAVPDSWPFHHPVNKKFVPDYYKVIVNPMDLETIRKNISKHKYQSRESFLDDVNLILA NSVKYNGPESQYTKTAQEIVNVCYQTLTEYDEHLTQLEKDICTAKEAALEEA
>3AAD_2 Histone chaperone ASF1A (chains B, D) GSHMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVL DSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEY TETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED
Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction. Akai, Y., Adachi, N., Hayashi, Y. et al. Proc Natl Acad Sci U S A (2010) 107:8153-8158. DOI 10.1073/pnas.0912509107 · PubMed
Other PDB entries of the same protein (UniProt P21675 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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