4QYL: Human BRPF1 bromodomain

Crystal Structure of the human BRPF1 bromodomain in complex with a histone H2AK5ac peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 24 Sept 2014.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
8
Atoms
4,989
Mol. weight
60.14 kDa
Released
24 Sept 2014

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

Secondary structure: helices and β-sheets

4QYL contains 20 α-helices and 0 β-strands across 4 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.

Chains A and C: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix7-2216
α-helix40-434
α-helix50-589
α-helix65-8218
α-helix88-11326
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix7-2216
α-helix40-434
α-helix50-5910
α-helix65-8218
α-helix88-11326
Chain D: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix7-2115
α-helix40-434
α-helix50-589
α-helix65-8218
α-helix88-11326

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PeregrinA, B, C, Dprotein117Homo sapiensP55201 (AlphaFold model)
Histone H2A type 1E, F, G, Hprotein12Homo sapiensP0C0S8 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4QYL_1 Peregrin (chains A, B, C, D)
GPLQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAY
RYLNFDDFEEDFNLIVSNCLKYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMGID
Sequence of entity 2 (E, F, G, H), FASTA
>4QYL_2 Histone H2A type 1 (chains E, F, G, H)
SGRGKQGGKARA

Primary citation

Structural insights into recognition of acetylated histone ligands by the BRPF1 bromodomain. Lubula, M.Y., Eckenroth, B.E., Carlson, S. et al. FEBS Lett (2014) 588:3844-3854. DOI 10.1016/j.febslet.2014.09.028 · PubMed

Other PDB entries of the same protein (UniProt P55201 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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