PDBe 4oq3

X-ray diffraction
2.3Å resolution

Tetra-substituted imidazoles as a new class of inhibitors of the p53-MDM2 interaction

Released:

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase Mdm2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 96 amino acids
Theoretical weight: 11.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00987 (Residues: 17-111; Coverage: 19%)
  • Best match: Q00987-8 (Residues: 1-50)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 33.814Å b: 165.528Å c: 34.236Å
α: 90° β: 95.06° γ: 90°
R-values:
R R work R free
0.196 0.194 0.224
Expression system: Escherichia coli