› 5ms4

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129925 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Kallikrein-8 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 228 amino acids
Theoretical weight: 24.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60259 (Residues: 33-260; Coverage: 98%)
Gene names: KLK8, NRPN, PRSS19, TADG14, UNQ283/PRO322
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
LEUPEPTIN Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand TBU 3 x TBU
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 83.103Å b: 46.045Å c: 103.349Å
α: 90° β: 91.4° γ: 90°
R-values:
R R work R free
0.239 0.212 0.259
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Surface loops of trypsin-like serine proteases as determinants of function.
Goettig et al. (2019)
2 other articles

3 mentions without citation

Identification and pharmaceutical evaluation of novel frog skin-derived serine proteinase inhibitor peptide-PE-BBI (Pelophylax esculentus Bowman-Birk inhibitor) for the potential treatment of cancer.
Lyu et al. (2018)
2 more