PDBe 2v53

X-ray diffraction
3.2Å resolution

Crystal structure of a SPARC-collagen complex

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of sequence-specific collagen recognition by SPARC.
Proc. Natl. Acad. Sci. U.S.A. 105 18273-7 (2008)
PMID: 19011090

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SPARC Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 26.63 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: NEW P09486 (Residues: 70-303; Coverage: 79%)
Gene names: ON, SPARC
Sequence domains:
Structure domains:
Collagen alpha-1(III) chain Chains: B, C, D
Molecule details ›
Chains: B, C, D
Length: 33 amino acids
Theoretical weight: 3.07 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P02461 (Residues: 552-590; Coverage: 2%)
Gene name: COL3A1

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P42212
Unit cell:
a: 89.79Å b: 89.79Å c: 127.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.261 0.254 0.32
Expression systems:
  • Homo sapiens
  • Not provided