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Crystal complex of p53-V272M and antimony ion

Analyse Crystal complex of p53-V272M and antimony ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EAX
Type
protein
Length
774 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.55
Source
Homo sapiens
Molecule
Cellular tumor antigen p53
UniProt
P04637
Ligands
ZN, SB
Pockets
10 · best druggability 0.71

Structure

x-ray diffraction · resolution 2.55 · 2 distinct chains · 9% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CCellular tumor antigen p53protein1949% helix, 34% strandP04637
B, DCellular tumor antigen p53protein1939% helix, 34% strandP04637

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
  • SB · Antimony (III) 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110580.710.75129empty
26310.650.7579empty
3690.440.8221empty
4910.370.7620empty
5760.370.7719empty

Interfaces

5 interfaces between chains.

  • C–D · 604 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 590 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 428 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 193 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 12 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7EAX · Crystal complex of P53-V272M and antimony ion · the same entry in another collection · chain A against A, TM-score 1.00

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