MolNFT v1 · #146784 · protein
Crystal structure of P300 zz domain in complex with histone H3 peptide
6DS6 · Histone H3 peptide-histone acetyltransferase P300 chimeric…: “Crystal structure of P300 zz domain in complex with histone H3 peptide”. X-ray diffraction, 2 ligands (ZN, CL). MolNFT v1 #146784 on GenesisL1: 3D structure, binding…
- 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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