› 1ekb

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb1ekb/pdb
PDB entry 1ekb coloured by chain, front view.
PDB entry 1ekb coloured by chain, side view.
PDB entry 1ekb coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide.
Lu D, Fütterer K, Korolev S, Zheng X, Tan K, Waksman G, Sadler JE
J Mol Biol 292 361-73 (1999)
PMID: 10493881

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
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)
UniProt:
  • Canonical: P98072 (Residues: 788-800; Coverage: 1%)
Gene names: ENTK, PRSS7, TMPRSS15
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)
UniProt:
  • Canonical: P98072 (Residues: 801-1035; Coverage: 23%)
Gene names: ENTK, PRSS7, TMPRSS15
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
VAL-ASP-ASP-ASP-ASP-LYK PEPTIDE Chain: C
Molecule details ›
Chain: C
Length: 7 amino acids
Theoretical weight: 740 Da

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
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 system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Membrane-anchored serine proteases in health and disease.
Antalis et al. (2011)
3 more

14 mentions without citation

Structural basis for complement factor I control and its disease-associated sequence polymorphisms.
Roversi et al. (2011)
13 more