PDBe 4xxb

X-ray diffraction
2.4Å resolution

Crystal structure of human MDM2-RPL11

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
60S ribosomal protein L11 Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62913 (Residues: 1-178; Coverage: 100%)
Gene name: RPL11
Sequence domains:
E3 ubiquitin-protein ligase Mdm2 Chain: B
Molecule details ›
Chain: B
Length: 148 amino acids
Theoretical weight: 16.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00987 (Residues: 290-437; Coverage: 30%)
Gene name: MDM2
Sequence domains: Zn-finger in Ran binding protein and others
Structure domains: Rubrerythrin, domain 2

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P3221
Unit cell:
a: 58.307Å b: 58.307Å c: 115.129Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.227
Expression system: Escherichia coli