› 2axi

X-ray diffraction
1.4Å 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

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-162634 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Mdm2 Chain: A
Molecule details ›
Chain: A
Length: 115 amino acids
Theoretical weight: 13.36 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
cyclic 8-mer peptide Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.4 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand MPO 1 x MPO
2 modified residues:
Ligand 6CW 1 x 6CW
Ligand DPR 1 x DPR

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2221
Unit cell:
a: 45.18Å b: 77.749Å c: 61.257Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 not available 0.234
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

13 review citations

Aromatic rings in chemical and biological recognition: energetics and structures.
Salonen et al. (2011)
12 more

13 mentions without citation

Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.
Pelay-Gimeno et al. (2015)
12 more