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Crystal structure of the MDM2-mdmx ring domain heterodimer

Analyse Crystal structure of the MDM2-mdmx ring domain heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2VJF
Type
protein
Length
254 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase MDM2; MDM4 protein
EC
6.3.2.-
UniProt
Q00987, O15151
Ligands
ZN
Pockets
1 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CE3 ubiquitin-protein ligase MDM2 (EC 6.3.2.-)protein6420% helix, 27% strandQ00987
B, DMDM4 proteinprotein6321% helix, 32% strandO15151

Ligands and binding sites

  • ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
  • FLC · Citrate anion · additive · chains D

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11490.430.7523empty

Interfaces

4 interfaces between chains.

  • A–B · 1369 Ų buried · 16 hydrogen bonds · protein-protein
  • C–D · 1356 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 191 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 160 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 2VJF · Crystal Structure of the MDM2-MDMX RING Domain Heterodimer · the same entry in another collection · chain A against A, TM-score 1.00
  • O15151 · AlphaFold monomer V2.0 prediction for protein MDM4 (O15151) · a predicted model of the same protein · chain B against A, TM-score 0.92

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