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Human P53 core domain with hot spot mutation R273C

Analyse Human P53 core domain with hot spot mutation R273C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4IBQ
Type
protein
Length
770 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 0.72

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CCellular tumor antigen P53protein1929% helix, 34% strandP04637
B, DCellular tumor antigen P53protein1938% helix, 34% strandP04637

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A, D
  • ACT · Acetate ion · additive · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19970.720.76125empty
23730.570.7553empty
31600.470.7631empty
41600.420.7437empty
5640.420.8217EDO

Interfaces

5 interfaces between chains.

  • B–C · 543 Ų buried · 5 hydrogen bonds · protein-protein
  • A–D · 499 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 401 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 237 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 32 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4IBQ · Human p53 core domain with hot spot mutation R273C · the same entry in another collection · chain A against A, TM-score 1.00

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