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Human P53 core domain mutant N235K

Analyse Human P53 core domain mutant N235K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LO9
Type: protein
Length: 776 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular tumor antigen P53
UniProt: P04637
Ligands: ZN
Pockets: 7 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cellular tumor antigen P53	protein	194	9% helix, 35% strand	P04637

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B, C, D

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

Pockets

7 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	313	0.61	0.78	40	empty
2	89	0.42	0.78	17	empty
3	115	0.39	0.75	19	empty
4	98	0.37	0.75	19	empty
5	86	0.36	0.76	19	empty

Interfaces

2 interfaces between chains.

B–D · 508 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 308 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4LO9 · Human p53 Core Domain Mutant N235K · 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 4LO9 · PDBe 4LO9 · UniProt P04637

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