› 4fqn

X-ray diffraction
1.9Å resolution

Crystal structure of the CCM2 C-terminal Harmonin Homology Domain (HHD)

Released:
DOI: 10.2210/pdb4fqn/pdb
PDB entry 4fqn coloured by chain, front view.
PDB entry 4fqn coloured by chain, side view.
PDB entry 4fqn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus.
Fisher OS, Zhang R, Li X, Murphy JW, Demeler B, Boggon TJ
FEBS Lett 587 272-7 (2013)
PMID: 23266514

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cerebral cavernous malformations 2 protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 98 amino acids
Theoretical weight: 11.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BSQ5 (Residues: 283-379; Coverage: 22%)
Gene names: C7orf22, CCM2, PP10187
Sequence domains: Cerebral cavernous malformation protein, harmonin-homology
Structure domains: Paired amphipathic helix 2 (pah2 repeat)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 62.166Å b: 64.196Å c: 89.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.219
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Cerebral cavernous malformation proteins at a glance.
Draheim et al. (2014)
8 more

9 mentions without citation

αα-Hub domains and intrinsically disordered proteins: A decisive combo.
Bugge et al. (2021)
8 more