› 1eaw

X-ray diffraction
2.93Å resolution

Crystal structure of the MTSP1 (matriptase)-BPTI (aprotinin) complex

Released:
DOI: 10.2210/pdb1eaw/pdb
PDB entry 1eaw coloured by chain, front view.
PDB entry 1eaw coloured by chain, side view.
PDB entry 1eaw coloured by chain, top view.
Source organisms:
Primary publication:
Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase.
Friedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL
J Biol Chem 277 2160-8 (2002)
PMID: 11696548

Function and Biology Details

Reaction catalysed: 
Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133760 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Suppressor of tumorigenicity 14 protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 241 amino acids
Theoretical weight: 26.46 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q9Y5Y6 (Residues: 615-855; Coverage: 28%)
Gene names: PRSS14, SNC19, ST14, TADG15
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor Chains: B, D
Molecule details ›
Chains: B, D
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 47.099Å b: 54.233Å c: 67.824Å
α: 107.62° β: 96.86° γ: 103.36°
R-values:
R R work R free
0.199 0.199 0.279
Expression systems:
  • Saccharomyces cerevisiae
  • Escherichia coli

Quick links

Citations

9 review citations

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

32 mentions without citation

Mechanisms of macromolecular protease inhibitors.
Farady et al. (2010)
31 more