› 4axy

X-ray diffraction
1.24Å resolution

A molecular basis for the action of the collagen-specific chaperone Hsp47-SERPINH1 and its structure-specific client recognition.

Released:
DOI: 10.2210/pdb4axy/pdb
PDB entry 4axy coloured by chain, front view.
PDB entry 4axy coloured by chain, side view.
PDB entry 4axy coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition.
Widmer C, Gebauer JM, Brunstein E, Rosenbaum S, Zaucke F, Drögemüller C, Leeb T, Baumann U
Proc Natl Acad Sci U S A 109 13243-7 (2012)
PMID: 22847422

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
COLLAGEN-LIKE PEPTIDE Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 20 amino acids
Theoretical weight: 1.61 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P43212
Unit cell:
a: 45.67Å b: 45.67Å c: 34.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.173
Expression system: Not provided

Quick links

Citations

14 review citations

Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta.
Eyre et al. (2013)
13 more

6 mentions without citation

Persistent homology analysis of protein structure, flexibility, and folding.
Xia et al. (2014)
5 more