› 1t4f

X-ray diffraction
1.9Å 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 domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162457 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Mdm2 Chain: M
Molecule details ›
Chain: M
Length: 110 amino acids
Theoretical weight: 12.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q00987 (Residues: 16-125; Coverage: 22%)
Gene name: MDM2
Sequence domains: SWIB/MDM2 domain
Structure domains: SWIB/MDM2 domain
optimized p53 peptide Chain: P
Molecule details ›
Chain: P
Length: 9 amino acids
Theoretical weight: 1.22 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P212121
Unit cell:
a: 41.03Å b: 43.59Å c: 54.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.231
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

88 review citations

Reaching for high-hanging fruit in drug discovery at protein-protein interfaces.
Wells et al. (2007)
87 more

28 mentions without citation

Chemistry and biology of multicomponent reactions.
Dömling et al. (2012)
27 more