› 1sht

X-ray diffraction
1.81Å resolution

Crystal Structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor

Released:
DOI: 10.2210/pdb1sht/pdb
PDB entry 1sht coloured by chain, front view.
PDB entry 1sht coloured by chain, side view.
PDB entry 1sht coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor.
Lacy DB, Wigelsworth DJ, Scobie HM, Young JA, Collier RJ
Proc Natl Acad Sci U S A 101 6367-72 (2004)
PMID: 15079089

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anthrax toxin receptor 2 Chain: X
Molecule details ›
Chain: X
Length: 181 amino acids
Theoretical weight: 19.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P58335 (Residues: 38-217; Coverage: 40%)
Gene names: ANTXR2, CMG2
Sequence domains: von Willebrand factor type A domain
Structure domains: von Willebrand factor, type A domain

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P213
Unit cell:
a: 79.691Å b: 79.691Å c: 79.691Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.186
Expression system: Escherichia coli BL21(DE3)

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Citations

18 review citations

Anthrax toxin: receptor binding, internalization, pore formation, and translocation.
Young et al. (2007)
17 more

6 mentions without citation

Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor.
Lacy et al. (2004)
5 more