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Crystal structure of STH1 bromodomain in complex with H3K14AC

Analyse Crystal structure of STH1 bromodomain in complex with H3K14AC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KMJ
Type
protein
Length
129 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nuclear protein STH1/NPS1; Histone H3
EC
3.6.4.12
UniProt
P32597, P61830

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANuclear protein STH1/NPS1 (EC 3.6.4.12)protein11258% helix, 3% strandP32597
CHistone H3protein1724% helix, 6% strandP61830

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Interfaces

1 interface between chains.

  • A–C · 841 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

  • 6KMJ · Crystal structure of Sth1 bromodomain in complex with H3K14Ac · the same entry in another collection · chain A against A, TM-score 1.00
  • P32597 · AlphaFold monomer V2.0 prediction for nuclear protein STH1/NPS1 (P32597) · a predicted model of the same protein · chain A against A, TM-score 0.96
  • P61830 · AlphaFold monomer V2.0 prediction for histone H3 (P61830) · a predicted model of the same protein · chain C against A, TM-score 0.20

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