3q49

X-ray diffraction
1.54Å resolution

Crystal structure of the TPR domain of CHIP complexed with Hsp70-C 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-143654 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CHIP Chain: B
Molecule details ›
Chain: B
Length: 137 amino acids
Theoretical weight: 15.73 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WUD1 (Residues: 23-155; Coverage: 44%)
Gene names: Chip, Stub1
Sequence domains: Anaphase-promoting complex, cyclosome, subunit 3
Structure domains: Tetratricopeptide repeat domain
Heat shock 70 kDa protein 1A Chain: C
Molecule details ›
Chain: C
Length: 8 amino acids
Theoretical weight: 859 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P0DMV8 (Residues: 634-641; Coverage: 1%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 46.033Å b: 77.967Å c: 37.341Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.206
Expression systems:
  • Escherichia coli
  • Not provided