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Crystal structure of the first bromodomain (BD1) of human BRD2 bound to ERK5-IN-1

Analyse Crystal structure of the first bromodomain (BD1) of human BRD2 bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LAU
Type: protein
Length: 108 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.4
Source: Homo sapiens
Molecule: Bromodomain-containing protein 2
UniProt: U3KQA6
Ligands: VYJ
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · resolution 2.4 · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain-containing protein 2	protein	108	65% helix, 0% strand	U3KQA6

Ligands and binding sites

VYJ · 11-cyclopentyl-2-({2-ethoxy-4-[4-(4-methylpiperazin-1-yl)piperidine-1-carbonyl]phenyl}amino)-5-methyl-5,11-dihydro-6H-pyrimido[4,5-b][1,4]benzodiazepin-6-one · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	93	0.46	0.80	18	VYJ

Compared structures

7LAU · Crystal structure of the first bromodomain (BD1) of human BRD2 bound to ERK5-in-1 · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt U3KQA6
Elsewhere: RCSB PDB 7LAU · PDBe 7LAU · UniProt U3KQA6

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