4YYN: TAF1 BD2 Bromodomain

Crystal structure of TAF1 BD2 Bromodomain bound to a crotonyllysine peptide. Determined by X-ray diffraction at 1.85 Å resolution. Released 16 Sept 2015.

Method
X-ray diffraction
Resolution
1.85 Å
Organism
Homo sapiens
Chains
3
Atoms
2,295
Mol. weight
34.26 kDa
Released
16 Sept 2015

Explore 4YYN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4YYN contains 17 α-helices and 0 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.

Chain A: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix1502-151312
α-helix1514-15196
α-helix1526-15294
α-helix1540-15434
α-helix1550-15589
α-helix1565-158319
α-helix1588-160619
α-helix1608-162821
Chain B: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1503-151311
α-helix1514-15196
α-helix1526-15283
α-helix1531-15333
α-helix1540-15434
α-helix1550-15589
α-helix1565-158319
α-helix1588-160619
α-helix1608-162821

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription initiation factor TFIID subunit 1A, Bprotein144Homo sapiensP21675 (AlphaFold model)
Histone H4Zprotein11Homo sapiensP62805 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4YYN_1 Transcription initiation factor TFIID subunit 1 (chains A, B)
GSPLLDDDDQVAFSFILDNIVTQKMMAVPDSWPFHHPVNKKFVPDYYKVIVNPMDLETIR
KNISKHKYQSRESFLDDVNLILANSVKYNGPESQYTKTAQEIVNVCYQTLTEYDEHLTQL
EKDICTAKEAALEEAELESLDPMT
Sequence of entity 2 (Z), FASTA
>4YYN_2 Histone H4 (chains Z)
SGRGXGGXGLG

Primary citation

A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications. Flynn, E.M., Huang, O.W., Poy, F. et al. Structure (2015) 23:1801-1814. DOI 10.1016/j.str.2015.08.004 · PubMed

Other PDB entries of the same protein (UniProt P21675 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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