X-ray diffraction
2.55Å resolution

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


Function and Biology Details

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SERPIN domain-containing protein Chains: A, B, C, D, K, L, P, Q
Molecule details ›
Chains: A, B, C, D, K, L, P, Q
Length: 392 amino acids
Theoretical weight: 44.28 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21
  • Canonical: E2RHY7 (Residues: 36-418; Coverage: 96%)
Gene name: SERPINH1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
COLLAGEN MODEL PEPTIDE 18-T8R11 Chains: E, F, G, H, I, J, M, N, O, R, S, T
Molecule details ›
Chains: E, F, G, H, I, J, M, N, O, R, S, T
Length: 19 amino acids
Theoretical weight: 1.56 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P2
Unit cell:
a: 102.709Å b: 104.905Å c: 171.84Å
α: 90° β: 103.71° γ: 90°
R R work R free
0.196 0.195 0.218
Expression systems:
  • Escherichia coli BL21
  • Not provided