4r0i

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE of MATRIPTASE in COMPLEX WITH INHIBITOR

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Suppressor of tumorigenicity 14 protein Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 26.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5Y6 (Residues: 615-855; Coverage: 28%)
Gene names: PRSS14, SNC19, ST14, TADG15
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Suppressor of tumorigenicity 14 protein Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 449 Da
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5Y6 (Residues: 604-607; Coverage: 1%)
Gene names: PRSS14, SNC19, ST14, TADG15

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C222
Unit cell:
a: 66.842Å b: 140.448Å c: 51.899Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.22 0.289
Expression system: Escherichia coli