› 7asc

X-ray diffraction
4.8Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172330 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transforming growth factor-beta-induced protein ig-h3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 594 amino acids
Theoretical weight: 65.12 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q15582 (Residues: 45-633; Coverage: 89%)
Gene names: BIGH3, TGFBI
Sequence domains: Fasciclin domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P41212
Unit cell:
a: 206.76Å b: 206.76Å c: 127.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.25 0.259
Expression system: Homo sapiens

Quick links

Citations

1 review citation

Clusterin, other extracellular chaperones, and eye disease.
Wilson et al. (2022)
2 other articles

1 mention without citation

Mutation-induced dimerization of transforming growth factor-β-induced protein may drive protein aggregation in granular corneal dystrophy.
Nielsen et al. (2021)