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Crystal structure of the first bromodomain (BD1) of human BRD2 bound to RO3280

Analyse Crystal structure of the first bromodomain (BD1) of human BRD2 bound to RO3280 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LAJ
Type: protein
Length: 122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bromodomain-containing protein 2
UniProt: U3KQA6
Ligands: 79C
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain-containing protein 2	protein	122	55% helix, 2% strand	U3KQA6

Ligands and binding sites

79C · 4-[(9-cyclopentyl-7,7-difluoro-5-methyl-6-oxo-6,7,8,9-tetrahydro-5H-pyrimido[4,5-b][1,4]diazepin-2-yl) amino]-3-methoxy-N-(1-methylpiperidin-4-yl)benzamide · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	99	0.50	0.81	18	79C

Compared structures

7LAJ · Crystal structure of the first bromodomain (BD1) of human BRD2 bound to Ro3280 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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 7LAJ · PDBe 7LAJ · UniProt U3KQA6

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