PDBe 1k9o

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX

Released:
Source organisms:
Primary publication:
The structure of a Michaelis serpin-protease complex.
Nat. Struct. Biol. 8 979-83 (2001)
PMID: 11685246

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alaserpin Chain: I
Molecule details ›
Chain: I
Length: 378 amino acids
Theoretical weight: 42.02 KDa
Source organism: Manduca sexta
Expression system: Escherichia coli
UniProt:
  • Canonical: P14754 (Residues: 15-392; Coverage: 100%)
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Anionic trypsin-2 Chain: E
Molecule details ›
Chain: E
Length: 223 amino acids
Theoretical weight: 23.8 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00763 (Residues: 24-246; Coverage: 97%)
Gene names: Prss2, Try2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3121
Unit cell:
a: 112.572Å b: 112.572Å c: 95.955Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.158 0.231
Expression systems:
  • Escherichia coli
  • Saccharomyces cerevisiae