› 5lpe

X-ray diffraction
2.65Å resolution

Kallikrein-related peptidase 10 complex with Zn2+

Released:
DOI: 10.2210/pdb5lpe/pdb
PDB entry 5lpe coloured by chain, front view.
PDB entry 5lpe coloured by chain, side view.
PDB entry 5lpe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the Zn2+ inhibition of the zymogen-like kallikrein-related peptidase 10.
Debela M, Magdolen V, Bode W, Brandstetter H, Goettig P
Biol Chem 397 1251-1264 (2016)
PMID: 27611765

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128874 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kallikrein-10 Chains: A, B
Molecule details ›
Chains: A, B
Length: 234 amino acids
Theoretical weight: 25.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43240 (Residues: 43-276; Coverage: 95%)
Gene names: KLK10, NES1, PRSSL1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand SO4 6 x SO4
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 52.914Å b: 67.037Å c: 57.768Å
α: 90° β: 104.37° γ: 90°
R-values:
R R work R free
0.223 0.22 0.278
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Surface loops of trypsin-like serine proteases as determinants of function.
Goettig et al. (2019)
1 more

2 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)
1 more