1r64

X-ray diffraction
2.2Å resolution

The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of -Lys-Arg-|- and -Arg-Arg-|- bonds to process yeast alpha-factor pheromone and killer toxin precursors.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146487 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Kexin Chains: A, B
Molecule details ›
Chains: A, B
Length: 481 amino acids
Theoretical weight: 52.64 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P13134 (Residues: 121-601; Coverage: 61%)
Gene names: KEX2, N1122, QDS1, YNL238W
Sequence domains:
Structure domains:
Ac-Arg-Glu-Lys-boroArg peptide inhibitor Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 amino acids
Theoretical weight: 616 Da
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P6522
Unit cell:
a: 113.541Å b: 113.541Å c: 364.971Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 0.234
Expression systems:
  • Saccharomyces cerevisiae
  • Not provided