1ekb

X-ray diffraction
2.3Å resolution

THE SERINE PROTEASE DOMAIN OF ENTEROPEPTIDASE BOUND TO INHIBITOR VAL-ASP-ASP-ASP-ASP-LYS-CHLOROMETHANE

Released:
Model geometry
Fit model/data
Data not deposited

Function and Biology Details

Reaction catalysed:
Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-161342 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Enteropeptidase non-catalytic heavy chain Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.42 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
Enteropeptidase catalytic light chain Chain: B
Molecule details ›
Chain: B
Length: 235 amino acids
Theoretical weight: 26.28 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
VAL-ASP-ASP-ASP-ASP-LYK PEPTIDE Chain: C

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 39.99Å b: 70.65Å c: 85.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.269
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided