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Human P53 core domain mutant M133L-V203A-N239Y-N268D-R273C

Analyse Human P53 core domain mutant M133L-V203A-N239Y-N268D-R273C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J20
Type: protein
Length: 389 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular tumor antigen P53
UniProt: P04637
Ligands: ZN, SO4
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellular tumor antigen P53	protein	195	8% helix, 33% strand	P04637
B	Cellular tumor antigen P53	protein	194	8% helix, 34% strand	P04637

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

4 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	390	0.62	0.77	43	empty
2	139	0.42	0.75	20	empty
3	96	0.36	0.75	19	empty
4	73	0.34	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 281 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2J20 · Human p53 core domain mutant M133L-V203A-N239Y-N268D-R273C · 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 2J20 · PDBe 2J20 · UniProt P04637

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