PDBe 3g03

X-ray diffraction
1.8Å resolution

Structure of human MDM2 in complex with high affinity peptide

Released:
Source organism: Homo sapiens
Primary publication:
Hot, hotter, hottest.
Cell Cycle 8 1112 (2009)
PMID: 19342883

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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Mdm2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 109 amino acids
Theoretical weight: 12.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00987 (Residues: 18-125; Coverage: 22%)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain
High affinity synthetic peptide Chains: B, D
Molecule details ›
Chains: B, D
Length: 12 amino acids
Theoretical weight: 1.5 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 44.36Å b: 60.17Å c: 71.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.268
Expression systems:
  • Escherichia coli
  • Not provided