ISDA: 5C85

Deposition Date 2015-06-25

Release Date 2016-05-25

Last Version Date 2024-01-10

Entry Detail

PDB ID:

5C85

Keywords:

DNA BINDING PROTEIN

Title:

Crystal structure of the human BRPF1 bromodomain in complex with SEED1

Biological Source:

Source Organism(s):

Homo sapiens (Taxon ID: 9606)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.70 Å

R-Value Free:

0.22

R-Value Work:

0.20

R-Value Observed:

0.20

Space Group:

P 32 2 1

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Peregrin
Gene (Uniprot):BRPF1
Chain IDs:A
Chain Length:116
Number of Molecules:1
Biological Source:Homo sapiens

UniProt ID:P55201 Pfam ID:PF00439

Ligand Molecules

4YO

NO3

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.Show

J. Med. Chem. 59 5555 5561 (2016)

PMID: 27167503 DOI: 10.1021/acs.jmedchem.6b00215

Abstact

BRPF1 plays a scaffolding role in transcription. We report on fragment screening by high-throughput docking to the BRPF1 bromodomain which resulted in six chemotypes with very favorable ligand efficiency (0.45-0.50 kcal/mol per non-hydrogen atom). Twenty crystal structures of BRPF1/ligand complexes show structural conservation in the acetyllysine binding site, common binding motifs, and unusual interactions (e.g., the replacement of a conserved water molecule). The structural information is useful for the design of chemical probes.

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Primary Citation of related structures

Abstact

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