› 3q47

X-ray diffraction
1.7Å resolution

Crystal structure of TPR domain of CHIP complexed with pseudophosphorylated Smad1 peptide

Released:
DOI: 10.2210/pdb3q47/pdb
PDB entry 3q47 coloured by chain, front view.
PDB entry 3q47 coloured by chain, side view.
PDB entry 3q47 coloured by chain, top view.
Source organisms:
Primary publication:
Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP).
Wang L, Liu YT, Hao R, Chen L, Chang Z, Wang HR, Wang ZX, Wu JW
J Biol Chem 286 15883-94 (2011)
PMID: 21454478

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172410 (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
Mothers against decapentaplegic homolog 1 Chain: C
Molecule details ›
Chain: C
Length: 10 amino acids
Theoretical weight: 1.08 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15797 (Residues: 456-464; Coverage: 2%)
Gene names: BSP1, MADH1, MADR1, SMAD1

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: 46.01Å b: 77.411Å c: 36.113Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.192
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

13 review citations

TGF-β and BMP signaling in osteoblast differentiation and bone formation.
Chen et al. (2012)
12 more

2 mentions without citation

Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP).
Wang et al. (2011)
1 more