› 1k9o

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX

Released:
DOI: 10.2210/pdb1k9o/pdb
PDB entry 1k9o coloured by chain, front view.
PDB entry 1k9o coloured by chain, side view.
PDB entry 1k9o coloured by chain, top view.
Source organisms:
Primary publication:
The structure of a Michaelis serpin-protease complex.
Ye S, Cech AL, Belmares R, Bergstrom RC, Tong Y, Corey DR, Kanost MR, Goldsmith EJ
Nat Struct Biol 8 979-83 (2001)
PMID: 11685246

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133400 (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

Quick links

Citations

21 review citations

The protein structures that shape caspase activity, specificity, activation and inhibition.
Fuentes-Prior et al. (2004)
20 more

20 mentions without citation

Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions.
Whisstock et al. (2010)
19 more