7F3S: Sth1 Bromodomain

Crystal structure of Sth1 Bromodomain in complex with H3K14bz peptide. Determined by X-ray diffraction at 1.4 Å resolution. Released 16 Mar 2022.

Method
X-ray diffraction
Resolution
1.4 Å
Organisms
Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Saccharomyces cerevisiae
Chains
2
Atoms
1,193
Mol. weight
15.46 kDa
Released
16 Mar 2022

Explore 7F3S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7F3S contains 10 α-helices and 4 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.

Chain A: 8 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix1252-126312
β-strand126611
β-strand127311
α-helix1276-12783
α-helix1281-12833
α-helix1290-12934
α-helix1300-13089
α-helix1315-133218
β-strand133312
α-helix13341
α-helix1338-135619
Chain B: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix7-93
β-strand1612
α-helix18-225

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nuclear protein STH1/NPS1Aprotein112Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P32597 (AlphaFold model)
Thr-ala-arg-lys-ser-thr-gly-gly-lbz-ala-pro-arg-lys-gln-leu-ala-ser-tyrBprotein18Saccharomyces cerevisiaeP61830 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7F3S_1 Nuclear protein STH1/NPS1 (chains A)
SLGIFPTVEKLVEEMREQLDEVDSHPRTSIFEKLPSKRDYPDYFKVIEKPMAIDIILKNC
KNGTYKTLEEVRQALQTMFENARFYNEEGSWVYVDADKLNEFTDEWFKEHSS
Sequence of entity 2 (B), FASTA
>7F3S_2 THR-ALA-ARG-LYS-SER-THR-GLY-GLY-LBZ-ALA-PRO-ARG-LYS-GLN-LEU-ALA-SER-TYR (chains B)
TARKSTGGKAPRKQLASY

Primary citation

Global profiling of regulatory elements in the histone benzoylation pathway. Wang, D., Yan, F., Wu, P. et al. Nat Commun (2022) 13:1369-1369. DOI 10.1038/s41467-022-29057-2 · PubMed

Other PDB entries of the same protein (UniProt P32597 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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