› 1rv1

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF HUMAN MDM2 WITH AN IMIDAZOLINE INHIBITOR

Released:
DOI: 10.2210/pdb1rv1/pdb
PDB entry 1rv1 coloured by chain, front view.
PDB entry 1rv1 coloured by chain, side view.
PDB entry 1rv1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
In vivo activation of the p53 pathway by small-molecule antagonists of MDM2.
Vassilev LT, Vu BT, Graves B, Carvajal D, Podlaski F, Filipovic Z, Kong N, Kammlott U, Lukacs C, Klein C, Fotouhi N, Liu EA
Science 303 844-8 (2004)
PMID: 14704432

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 domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase Mdm2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 85 amino acids
Theoretical weight: 10.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q00987 (Residues: 25-109; Coverage: 17%)
  • Best match: Q00987-8 (Residues: 1-48)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain

Ligands and Environments

1 bound ligand:
Ligand IMZ 5 x IMZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2
Unit cell:
a: 122.264Å b: 39.727Å c: 79.362Å
α: 90° β: 114.29° γ: 90°
R-values:
R R work R free
0.266 0.256 0.322
Expression system: Escherichia coli BL21

Quick links

Citations

748 review citations

Blinded by the Light: The Growing Complexity of p53.
Vousden et al. (2009)
747 more

52 mentions without citation

Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy.
Shangary et al. (2009)
51 more