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Crystal structure of the TAZ2 domain of P300

Analyse Crystal structure of the TAZ2 domain of P300 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IO2
Type: protein
Length: 109 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase P300
EC: 2.3.1.48
UniProt: Q09472
Ligands: ZN, SO4

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase P300 (EC 2.3.1.48)	protein	109	71% helix, 0% strand	Q09472

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A

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

Compared structures

3IO2 · Crystal structure of the Taz2 domain of p300 · 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 0.79

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 3IO2 · PDBe 3IO2 · UniProt Q09472

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