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Crystal structure of the human P53 core domain mutant M133L/V203A/N239Y/N268D at 1.9 a resolution.

Analyse Crystal structure of the human P53 core domain mutant M133L/V203A/N239Y/N268D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UOL
Type: protein
Length: 390 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular tumor antigen P53
UniProt: P04637
Ligands: ZN
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cellular tumor antigen P53	protein	195	8% helix, 33% strand	P04637

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

3 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	475	0.65	0.78	58	empty
2	160	0.44	0.75	20	empty
3	115	0.38	0.74	22	empty

Interfaces

1 interface between chains.

A–B · 300 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1UOL · Crystal structure of the human p53 core domain mutant M133L/V203A/N239Y/N268D at 1.9 A… · the same entry in another collection · chain A against A, TM-score 1.00

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 1UOL · PDBe 1UOL · UniProt P04637

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