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Structural basis for the regulation of P53 function by P300

Analyse Structural basis for the regulation of P53 function by P300 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2K8F
Type: protein
Length: 129 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase P300; Cellular tumor antigen P53
EC: 2.3.1.48
UniProt: Q09472, P04637
Pockets: 2 · best druggability 0.41

Structure

solution nmr · 2 distinct chains · 54% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase P300 (EC 2.3.1.48)	protein	90	69% helix, 0% strand	Q09472
B	Cellular tumor antigen P53	protein	39	21% helix, 0% strand	P04637

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.41	0.78	23	empty
2	91	0.38	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 982 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2K8F · Structural Basis for the Regulation of p53 Function by 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 0.76

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
Every structure of UniProt P04637
Elsewhere: RCSB PDB 2K8F · PDBe 2K8F · UniProt Q09472 · UniProt P04637

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