2gv2

X-ray diffraction
1.8Å resolution

MDM2 in complex with an 8-mer p53 peptide analogue

Released:
Source organism: Homo sapiens
Primary publication:
Crystallographic analysis of an 8-mer p53 peptide analogue complexed with MDM2.
J Am Chem Soc 128 11000-1 (2006)
PMID: 16925398

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-162724 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Mdm2 Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00987 (Residues: 17-125; Coverage: 22%)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain
8-MER P53 PEPTIDE ANALOGUE Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1.19 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
4 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 41.66Å b: 44.1Å c: 59.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.219
Expression systems:
  • Escherichia coli
  • Not provided