3AAD: Transcription initiation factor TFIID subunit 1

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.

Method
X-ray diffraction
Resolution
3.3 Å
Organism
Homo sapiens
Chains
3
Atoms
4,617
Mol. weight
70.22 kDa
Released
28 Apr 2010

Explore 3AAD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 18 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix1381-139616
α-helix1403-14053
α-helix1417-14204
α-helix1427-14359
α-helix1442-145918
α-helix1465-14706
α-helix1472-14754
α-helix1481-14833
α-helix1485-14939
α-helix1502-151312
α-helix1514-15185
α-helix1519-15213
α-helix1526-15283
α-helix1531-15333
α-helix1540-15434
α-helix1550-15589
α-helix1565-158319
α-helix1588-162740
Chain B: 4 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand4-851
β-strand1111
β-strand16-1722
α-helix211
β-strand22-3091
β-strand40-4562
β-strand55-6062
β-strand68-7691
α-helix77-793
α-helix81-833
β-strand92-101102
β-strand104-117142
α-helix132-1343
β-strand135-13952
β-strand145-14842
Chain D: 3 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand4-633
β-strand1114
β-strand16-1725
α-helix211
β-strand22-2434
β-strand27-3043
β-strand39-4465
β-strand55-6065
β-strand68-7143
β-strand74-7634
α-helix77-793
α-helix81-833
β-strand91-101115
β-strand104-117145
β-strand135-13955
β-strand145-14735

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription initiation factor TFIID subunit 1Aprotein292Homo sapiensP21675 (AlphaFold model)
Histone chaperone ASF1AB, Dprotein158Homo sapiensQ9Y294 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3AAD_1 Transcription initiation factor TFIID subunit 1 (chains A)
GSHMVLKFPKQQLPPKKKRRVGTTVHCDYLNRPHKSIHRRRTDPMVTLSSILESIINDMR
DLPNTYPFHTPVNAKVVKDYYKIITRPMDLQTLRENVRKRLYPSREEFREHLELIVKNSA
TYNGPKHSLTQISQSMLDLCDEKLKEKEDKLARLEKAINPLLDDDDQVAFSFILDNIVTQ
KMMAVPDSWPFHHPVNKKFVPDYYKVIVNPMDLETIRKNISKHKYQSRESFLDDVNLILA
NSVKYNGPESQYTKTAQEIVNVCYQTLTEYDEHLTQLEKDICTAKEAALEEA
Sequence of entity 2 (B, D), FASTA
>3AAD_2 Histone chaperone ASF1A (chains B, D)
GSHMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVL
DSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEY
TETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED

Primary citation

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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