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X-ray structure of Mdm2 with modified p53 peptide

Analyse X-ray structure of Mdm2 with modified p53 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7AD0
Type
protein
Length
602 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.07
Source
Homo sapiens; SYNTHETIC CONSTRUCT
Molecule
E3 ubiquitin-protein ligase Mdm2; Modified p53 peptide
EC
2.3.2.27
UniProt
Q00987
Pockets
7 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.07 · 4 distinct chains · 44% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27)protein9041% helix, 16% strandQ00987
B, D, E, FE3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27)protein8745% helix, 18% strandQ00987
CE3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27)protein8645% helix, 19% strandQ00987
H, I, J, K, L, MModified p53 peptideprotein1354% helix, 0% strand—

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11180.690.9121empty
24840.670.7844empty
31410.600.8423empty
41120.430.7719empty
5840.380.7619empty

Interfaces

16 interfaces between chains.

  • A–C · 664 Ų buried · 11 hydrogen bonds · protein-protein
  • A–H · 632 Ų buried · 4 hydrogen bonds · protein-protein
  • D–K · 631 Ų buried · 4 hydrogen bonds · protein-protein
  • B–I · 626 Ų buried · 5 hydrogen bonds · protein-protein
  • C–J · 626 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (nonstandard).

Compared structures

  • 7AD0 · X-ray structure of MDM2 with modified P53 peptide · the same entry in another collection · chain A against A, TM-score 1.00

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