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Lysine 120-acetylated P53 DNA binding domain in a complex with DNA.

Analyse Lysine 120-acetylated P53 DNA binding domain in a complex with DNA. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BUA
Type: protein + DNA
Length: 210 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular tumor antigen P53; DNA (5'-D(P*GP*GP*AP*CP*AP*TP*GP*TP*CP*C)-3')
UniProt: P04637
Ligands: ZN
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellular tumor antigen P53	protein	200	10% helix, 34% strand	P04637
B	DNA (5'-D(PGPGPAPCPAPTPGPTPCPC)-3')	dna	10	—	—

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.40	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 323 Å² buried · 7 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 1 modified (acetylation).

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
Elsewhere: RCSB PDB 5BUA · PDBe 5BUA · UniProt P04637

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