› 5trf

X-ray diffraction
2.1Å resolution

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
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-169499 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase Mdm2 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 109 amino acids
Theoretical weight: 12.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00987 (Residues: 10-118; Coverage: 22%)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain

Ligands and Environments

3 bound ligands:
Ligand 7HC 5 x 7HC
Ligand SO4 3 x SO4
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P43212
Unit cell:
a: 138.849Å b: 138.849Å c: 83.707Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.208
Expression system: Escherichia coli

Quick links

Citations

49 review citations

The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches.
Joerger et al. (2016)
48 more

13 mentions without citation

Small-molecule MDM2/X inhibitors and PROTAC degraders for cancer therapy: advances and perspectives.
Fang et al. (2020)
12 more