7UG5: Bromodomain-containing protein 3

Second bromodomain of BRD3 liganded with BMS-536924. Determined by X-ray diffraction at 1.8 Å resolution. Released 5 Apr 2023.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,346
Mol. weight: 54.31 kDa
Ligands: N6I
Released: 5 Apr 2023

Explore 7UG5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7UG5 contains 36 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.

Chain A: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	308-322	15
α-helix	325-327	3
α-helix	328-331	4
α-helix	332-334	3
α-helix	340-343	4
α-helix	348-351	4
α-helix	358-366	9
α-helix	373-390	18
α-helix	396-413	18

Chain B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	307-309	3
α-helix	310-322	13
α-helix	325-327	3
α-helix	328-331	4
α-helix	332-334	3
α-helix	340-343	4
α-helix	348-351	4
α-helix	358-366	9
α-helix	373-390	18
α-helix	396-413	18

Chain C: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	310-322	13
α-helix	325-327	3
α-helix	328-331	4
α-helix	332-334	3
α-helix	348-351	4
α-helix	358-366	9
α-helix	373-390	18
α-helix	396-413	18

Chain D: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	310-322	13
α-helix	325-327	3
α-helix	328-331	4
α-helix	332-334	3
α-helix	340-343	4
α-helix	348-351	4
α-helix	358-366	9
α-helix	373-390	18
α-helix	396-413	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bromodomain-containing protein 3	A, B, C, D	protein	111	Homo sapiens	Q15059 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>7UG5_1 Bromodomain-containing protein 3 (chains A, B, C, D)
GKLSEHLRYCDSILREMLSKKHAAYAWPFYKPVDAEALELHDYHDIIKHPMDLSTVKRKM
DGREYPDAQGFAADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMP

Ligands and cofactors

ID	Name	Formula	Copies
N6I	(3M)-4-{[(2S)-2-(3-chlorophenyl)-2-hydroxyethyl]amino}-3-[4-methyl-6-(morpholin…	C25 H26 Cl N5 O3	2

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

Primary citation

Structural basis of CBP and EP300 interaction with kinase inhibitors. Schonbrunn, E., Bikowitz, M. To be published.

Other PDB entries of the same protein (UniProt Q15059 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6QJU 1.2 Å, Crystal structure of human Bromodomain containing protein 3 (BRD3) in complex with…
3S92 1.36 Å, Crystal Structure of the second bromodomain of human BRD3 in complex with the inhibitor…
9NN4 1.37 Å, BET BRD3-BD1 in complex with peptide 7.2
2NXB 1.4 Å, Crystal structure of human Bromodomain containing protein 3 (BRD3)
7TOA 1.41 Å, BRD3-BD1 in complex with RaPID linear peptide 3xAcK.1 (triAcK.1)
7LAY 1.45 Å, Crystal structure of the first bromodomain (BD1) of human BRD3 bound to SG3-179
8CV5 1.47 Å, Peptide 4.2B in complex with BRD3.2
7L72 1.5 Å, Crystal structure of the second bromodomain (BD2) of human BRD3 bound to Ro3280
7RJL 1.5 Å, Crystal structure of human Bromodomain containing protein 3 (BRD3) in complex with SHMT
7TO8 1.5 Å, BRD3-BD1 in complex with RaPID linear peptide 2xAcK.1 (diAcK.1)
7L9L 1.55 Å, Crystal structure of the second bromodomain (BD2) of human BRD3 bound to BI2536
7TO9 1.6 Å, BRD3-BD1 in complex with RaPID linear peptide 2xAcK.4xE (diAcK.4xE)

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