5EVA: Human BRPF1 bromodomain

Crystal structure of the human BRPF1 bromodomain in complex with SEED16. Determined by X-ray diffraction at 1.45 Å resolution. Released 8 Jun 2016.

Method
X-ray diffraction
Resolution
1.45 Å
Organism
Homo sapiens
Chains
1
Atoms
1,108
Mol. weight
14 kDa
Ligands
5S9
Released
8 Jun 2016

Explore 5EVA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EVA contains 5 α-helices and 0 β-strands across 1 chain. 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: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix630-64718
α-helix665-6684
α-helix675-6839
α-helix690-70718
α-helix713-73826

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PeregrinAprotein116Homo sapiensP55201 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5EVA_1 Peregrin (chains A)
SMEMQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEA
YRYLNFDDFEEDFNLIVSNCLKYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMG

Ligands and cofactors

IDNameFormulaCopies
5S9~{N}-[2,4-bis(fluoranyl)phenyl]-2-methyl-pyrazole-3-carboxamideC11 H9 F2 N3 O1

Water and common crystallization additives (NO3) are not listed.

Primary citation

Twenty Crystal Structures of Bromodomain and PHD Finger Containing Protein 1 (BRPF1)/Ligand Complexes Reveal Conserved Binding Motifs and Rare Interactions. Zhu, J., Caflisch, A. J Med Chem (2016) 59:5555-5561. DOI 10.1021/acs.jmedchem.6b00215 · 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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