4nfe

X-ray diffraction
1.9Å resolution

Human kallikrein-related peptidase 2 in complex with benzamidine

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage of Arg-|- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|- or Leu-|-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|- bonds (5).
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kallikrein-2 Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 26.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20151 (Residues: 25-261; Coverage: 98%)
Gene name: KLK2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 59.65Å b: 60.39Å c: 67.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.213
Expression system: Escherichia coli