› 2w86

X-ray diffraction
1.8Å resolution

Crystal structure of fibrillin-1 domains cbEGF9hyb2cbEGF10, calcium saturated form

Released:
DOI: 10.2210/pdb2w86/pdb
PDB entry 2w86 coloured by chain, front view.
PDB entry 2w86 coloured by chain, side view.
PDB entry 2w86 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins.
Jensen SA, Iqbal S, Lowe ED, Redfield C, Handford PA
OpenAccess logo Structure 17 759-68 (2009)
PMID: 19446531

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152940 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibrillin-1 Chain: A
Molecule details ›
Chain: A
Length: 147 amino acids
Theoretical weight: 15.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P35555 (Residues: 807-951; Coverage: 5%)
Gene names: FBN, FBN1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand IOD 3 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 31.232Å b: 47.258Å c: 89.105Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.221
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Fibrillin microfibrils and elastic fibre proteins: Functional interactions and extracellular regulation of growth factors.
Thomson et al. (2019)
6 more

6 mentions without citation

Analysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modes.
Lössl et al. (2014)
5 more