6V1B: Bromodomain of human BRD9

Crystal structure of the bromodomain of human BRD9 bound to I-BRD9. Determined by X-ray diffraction at 1.35 Å resolution. Released 11 Mar 2020.

Method
X-ray diffraction
Resolution
1.35 Å
Organism
Homo sapiens
Chains
2
Atoms
2,275
Mol. weight
29.56 kDa
Ligands
H1B
Released
11 Mar 2020

Explore 6V1B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6V1B contains 14 α-helices and 0 β-strands across 2 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.

Chains A and B: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix140-15314
α-helix164-1663
α-helix173-1764
α-helix183-1919
α-helix198-21518
α-helix221-23616
α-helix239-24810

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bromodomain-containing protein 9A, Bprotein123Homo sapiensQ9H8M2 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6V1B_1 Bromodomain-containing protein 9 (chains A, B)
SMLKLSAENESTPIQQLLEHFLRQLQRKDPHGFFAFPVTDAIAPGYSMIIKHPMDFGTMK
DKIVANEYKSVTEFKADFKLMCDNAMTYNRPDTVYYKLAKKILHAGFKMMSKERLLALKR
SMS

Ligands and cofactors

IDNameFormulaCopies
H1BN'-[1,1-bis(oxidanylidene)thian-4-yl]-5-ethyl-4-oxidanylidene-7-[3-(trifluorome…C22 H22 F3 N3 O3 S22

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

Primary citation

Structural Basis of Inhibitor Selectivity in the BRD7/9 Subfamily of Bromodomains. Karim, R.M., Chan, A., Zhu, J.Y. et al. J Med Chem (2020) 63:3227-3237. DOI 10.1021/acs.jmedchem.9b01980 · PubMed

Other PDB entries of the same protein (UniProt Q9H8M2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 6V1B directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.