› 4erf

X-ray diffraction
2Å 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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-554040 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase Mdm2 Chains: A, C, E
Molecule details ›
Chains: A, C, E
Length: 96 amino acids
Theoretical weight: 11.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00987 (Residues: 17-111; Coverage: 19%)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain

Ligands and Environments

1 bound ligand:
Ligand 0R3 3 x 0R3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2221
Unit cell:
a: 56.77Å b: 97.89Å c: 105.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.25
Expression system: Escherichia coli

Quick links

Citations

23 review citations

MDM2, MDMX and p53 in oncogenesis and cancer therapy.
Wade et al. (2013)
22 more

9 mentions without citation

How To Design a Successful p53-MDM2/X Interaction Inhibitor: A Thorough Overview Based on Crystal Structures.
Estrada-Ortiz et al. (2016)
8 more