PDBe 3q4a

X-ray diffraction
1.54Å resolution

Crystal structure of the TPR domain of CHIP complexed with phosphorylated Smad1 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)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
STIP1 homology and U box-containing protein 1 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: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Mothers against decapentaplegic homolog 1 Chain: C
Molecule details ›
Chain: C
Length: 10 amino acids
Theoretical weight: 1.19 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15797 (Residues: 456-465; Coverage: 2%)
Gene names: BSP1, MADH1, MADR1, SMAD1

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 46.132Å b: 77.444Å c: 36.456Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.208
Expression systems:
  • Escherichia coli
  • Not provided