2id4

X-ray diffraction
1.9Å resolution

The 1.9 A structure of Kex2 in complex with an Ac-R-E-R-K-chloromethyl ketone inhibitor.

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2.
Proc Natl Acad Sci U S A 104 6626-31 (2007)
PMID: 17426142

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-146488 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Kexin Chains: A, B
Molecule details ›
Chains: A, B
Length: 503 amino acids
Theoretical weight: 55.18 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P13134 (Residues: 114-613; Coverage: 63%)
Gene names: KEX2, N1122, QDS1, YNL238W
Sequence domains:
Structure domains:
Ac-RERK-CMK inhibitor Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 650 Da
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, NDG
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P6522
Unit cell:
a: 112.851Å b: 112.851Å c: 370.165Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.206
Expression systems:
  • Saccharomyces cerevisiae
  • Not provided