Research workbench
Crystal structure of P300 zz domain in complex with histone H3 peptide
Analyse Crystal structure of P300 zz domain in complex with histone H3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DS6
- Type
- protein
- Length
- 53 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3 peptide-histone acetyltransferase P300 chimeric protein
- EC
- 2.3.1.48, 2.3.1.-
- UniProt
- Q09472
- Ligands
- ZN, CL
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H3 peptide-histone acetyltransferase P300 chimeric protein (EC 2.3.1.48, 2.3.1.-) | protein | 53 | 8% helix, 26% strand | Q09472 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DS6 · Crystal structure of p300 ZZ domain in complex with histone H3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q09472 · AlphaFold monomer V2.0 prediction for histone acetyltransferase P300 (Q09472) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 Q09472
- Elsewhere: RCSB PDB 6DS6 · PDBe 6DS6 · UniProt Q09472
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