PDBe 2fop

X-ray diffraction
2.1Å resolution

The Crystal Structure of the N-terminal domain of HAUSP/USP7 complexed with mdm2 peptide 147-150

Released:
Source organism: Homo sapiens
Primary publication:
Molecular recognition of p53 and MDM2 by USP7/HAUSP.
Nat. Struct. Mol. Biol. 13 285-91 (2006)
PMID: 16474402

Function and Biology Details

Reactions catalysed:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase 7 Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 18.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93009 (Residues: 54-205; Coverage: 14%)
Gene names: HAUSP, USP7
Sequence domains: MATH domain
Structure domains: Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
E3 ubiquitin-protein ligase Mdm2 Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 635 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q00987 (Residues: 145-150; Coverage: 1%)
Gene name: MDM2

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P41
Unit cell:
a: 69.9Å b: 69.9Å c: 45.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.25
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided