PDBe 3lnj

X-ray diffraction
2.4Å resolution

Crystal structure of human MDM2 in complex with D-peptide inhibitor (DPMI-alpha)

Released:
Source organism: Homo sapiens
Primary publication:
A left-handed solution to peptide inhibition of the p53-MDM2 interaction.
Angew. Chem. Int. Ed. Engl. 49 3649-52 (2010)
PMID: 20449836

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:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Mdm2 Chains: A, C, E
Molecule details ›
Chains: A, C, E
Length: 85 amino acids
Theoretical weight: 10.04 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q00987 (Residues: 25-109; Coverage: 17%)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain
D-peptide inhibitor Chains: B, D, F
Molecule details ›
Chains: B, D, F
Length: 12 amino acids
Theoretical weight: 1.52 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C2221
Unit cell:
a: 68.976Å b: 213.478Å c: 45.536Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.255
Expression system: Not provided