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Cryo-EM structure of P300-P53 protein complex

Analyse Cryo-EM structure of P300-P53 protein complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XZC
Type
protein
Length
1,547 residues
Chains
5
Method
electron microscopy
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
1 · best druggability 0.28

Structure

electron microscopy · 2 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone acetyltransferase P300 (EC 2.3.1.48)protein6190% helix, 0% strandQ09472
B, C, D, ECellular tumor antigen P53protein2320% helix, 0% strandP04637

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1520.280.7317empty

Interfaces

5 interfaces between chains.

  • B–D · 170 Ų buried · 0 hydrogen bonds · protein-protein
  • C–E · 170 Ų buried · 0 hydrogen bonds · protein-protein
  • D–E · 97 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 64 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 53 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5XZC · Cryo-EM structure of p300-p53 protein complex · the same entry in another collection · chain C against C, 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 0.59

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