› 4au3

X-ray diffraction
2.78Å resolution

Crystal Structure of a Hsp47-collagen complex

Released:
DOI: 10.2210/pdb4au3/pdb
PDB entry 4au3 coloured by chain, front view.
PDB entry 4au3 coloured by chain, side view.
PDB entry 4au3 coloured by chain, top view.
Source organisms:
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:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164292 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
SERPIN PEPTIDASE INHIBITOR, CLADE H (HEAT SHOCK PROTEIN 47 ), MEMBER 1, (COLLAGEN BINDING PROTEIN 1) Chains: A, C, D
Molecule details ›
Chains: A, C, D
Length: 392 amino acids
Theoretical weight: 44.89 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
Structure domains:
SERPYIN PEPTIDASE INHIBITOR, CLADE H (HEAT SHOCK PROTEIN 47 ), MEMBER 1, (COLLAGEN BINDING PROTEIN 1) Chain: B
Molecule details ›
Chain: B
Length: 392 amino acids
Theoretical weight: 44.91 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
Structure domains:
Collagen alpha-1(XXVI) chain Chains: E, F, G, H, I, J
Molecule details ›
Chains: E, F, G, H, I, J
Length: 20 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q96A83 (Residues: 309-326; Coverage: 4%)
Gene names: COL26A1, EMID2, EMU2

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 52 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P4122
Unit cell:
a: 101.26Å b: 101.26Å c: 366.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.203 0.234
Expression systems:
  • Escherichia coli BL21(DE3)
  • 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

5 mentions without citation

Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition.
Widmer et al. (2012)
4 more