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Crystal structure of the bromodomain of human SMARCA2

Analyse Crystal structure of the bromodomain of human SMARCA2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QY4
Type: protein
Length: 323 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SMARCA2 protein
UniProt: Q8N9Q1
Ligands: ZN
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 65% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SMARCA2 protein	protein	110	65% helix, 2% strand	Q8N9Q1
B	SMARCA2 protein	protein	108	67% helix, 2% strand	Q8N9Q1
C	SMARCA2 protein	protein	105	65% helix, 2% strand	Q8N9Q1

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A, B, C

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	822	0.70	0.76	60	empty
2	63	0.47	0.83	16	empty
3	66	0.43	0.81	13	empty

Interfaces

2 interfaces between chains.

A–B · 165 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 139 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4QY4 · Crystal structure of the bromodomain of human SMARCA2 · 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 Q8N9Q1
Elsewhere: RCSB PDB 4QY4 · PDBe 4QY4 · UniProt Q8N9Q1

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