Function and Biology Details
Reaction catalysed:
Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
Biochemical function:
Biological process:
- not assigned
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Radixin and Neprilysin (preferred)
PDBe Complex ID:
PDB-CPX-150652 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Radixin
Molecule details ›
Chains: A, B, C
Length: 312 amino acids
Theoretical weight: 36.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 312 amino acids
Theoretical weight: 36.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P26043 (Residues: 1-310; Coverage: 53%)
Sequence domains:
Structure domains:
Neprilysin
Molecule details ›
Chains: D, E, F
Length: 22 amino acids
Theoretical weight: 2.53 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
Length: 22 amino acids
Theoretical weight: 2.53 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
- Canonical: Q61391 (Residues: 2-23; Coverage: 3%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL41XU
Spacegroup:
P212121
Expression systems:
- Escherichia coli
- Not provided
