› 4nff

X-ray diffraction
1.9Å resolution

Human kallikrein-related peptidase 2 in complex with PPACK

Released:
DOI: 10.2210/pdb4nff/pdb
PDB entry 4nff coloured by chain, front view.
PDB entry 4nff coloured by chain, side view.
PDB entry 4nff coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity.
Skala W, Utzschneider DT, Magdolen V, Debela M, Guo S, Craik CS, Brandstetter H, Goettig P
J Biol Chem 289 34267-83 (2014)
PMID: 25326387

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148861 (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

1 bound ligand:
Ligand 0G6 1 x 0G6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P212121
Unit cell:
a: 60.1Å b: 60.74Å c: 66.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.232
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

3 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
2 more