Research workbench

P53-53BP2 complex

Analyse P53-53BP2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YCS
Type: protein
Length: 384 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P53; 53BP2
UniProt: P04637, Q13625
Ligands: ZN
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P53	protein	191	9% helix, 34% strand	P04637
B	53BP2	protein	193	37% helix, 13% strand	Q13625

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	394	0.62	0.78	55	empty
2	74	0.32	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 812 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1YCS · P53-53BP2 complex · the same entry in another collection · chain A against A, TM-score 1.00
Q13625 · AlphaFold monomer V2.0 prediction for apoptosis-stimulating of P53 protein 2 (Q13625) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P04637
Every structure of UniProt Q13625
Elsewhere: RCSB PDB 1YCS · PDBe 1YCS · UniProt P04637 · UniProt Q13625

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