Research workbench

Human P53 core domain mutant M133L-V203A-N239Y-N268D-R282W

Analyse Human P53 core domain mutant M133L-V203A-N239Y-N268D-R282W in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J21
Type: protein
Length: 376 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 0.68

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellular tumor antigen P53	protein	188	9% helix, 35% strand	P04637
B	Cellular tumor antigen P53	protein	188	7% helix, 35% 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	466	0.68	0.79	52	empty
2	138	0.43	0.76	21	empty
3	96	0.37	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 296 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2J21 · Human p53 core domain mutant M133L-V203A-N239Y-N268D-R282W · 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 2J21 · PDBe 2J21 · UniProt P04637

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