› 4wj7

X-ray diffraction
2.75Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165325 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cerebral cavernous malformations 2 protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 180 amino acids
Theoretical weight: 19.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BSQ5 (Residues: 51-228; Coverage: 40%)
Gene names: C7orf22, CCM2, PP10187
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
KRIT1 NPxY/F3 Chains: W, X, Y, Z
Molecule details ›
Chains: W, X, Y, Z
Length: 13 amino acids
Theoretical weight: 1.42 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P6522
Unit cell:
a: 110.938Å b: 110.938Å c: 315.255Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.22 0.25
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Introduction to cerebral cavernous malformation: a brief review.
Kim J. (2016)
3 more

3 mentions without citation

Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2) interaction with Krev interaction trapped 1 (KRIT1) by disease-associated mutations.
Fisher et al. (2015)
2 more