6nsv

X-ray diffraction
1.3Å resolution

Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated optimized peptide

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-167157 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CHIP Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UNE7 (Residues: 23-152; Coverage: 43%)
Gene names: CHIP, PP1131, STUB1
Sequence domains: Anaphase-promoting complex, cyclosome, subunit 3
ACE-LEU-TRP-TRP-PRO-ASP Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 742 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Unit cell:
a: 46.219Å b: 71.92Å c: 77.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.243
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided