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Crystal structure of human bromodomain containing 9 isoform 1 (BRD9)

Analyse Crystal structure of human bromodomain containing 9 isoform 1 (BRD9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HME
Type: protein
Length: 227 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bromodomain-containing protein 9
UniProt: Q9H8M2
Pockets: 4 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain-containing protein 9	protein	113	62% helix, 0% strand	Q9H8M2
B	Bromodomain-containing protein 9	protein	114	62% helix, 0% strand	Q9H8M2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.48	0.82	18	empty
2	77	0.42	0.79	17	empty
3	68	0.34	0.76	15	empty
4	53	0.30	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 876 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3HME · Crystal structure of human bromodomain containing 9 isoform 1 (BRD9) · the same entry in another collection · chain A against A, TM-score 1.00
Q9H8M2 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 9 (Q9H8M2) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q9H8M2
Elsewhere: RCSB PDB 3HME · PDBe 3HME · UniProt Q9H8M2

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