› 2anw

X-ray diffraction
1.85Å resolution

Expression, crystallization and three-dimensional structure of the catalytic domain of human plasma kallikrein: Implications for structure-based design of protease inhibitors

Released:
DOI: 10.2210/pdb2anw/pdb
PDB entry 2anw coloured by chain, front view.
PDB entry 2anw coloured by chain, side view.
PDB entry 2anw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Expression, crystallization, and three-dimensional structure of the catalytic domain of human plasma kallikrein.
Tang J, Yu CL, Williams SR, Springman E, Jeffery D, Sprengeler PA, Estevez A, Sampang J, Shrader W, Spencer J, Young W, McGrath M, Katz BA
J Biol Chem 280 41077-89 (2005)
PMID: 16199530

Function and Biology Details

Reaction catalysed: 
Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasma kallikrein light chain Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 27.1 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P03952 (Residues: 391-631; Coverage: 39%)
Gene names: KLK3, KLKB1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand BEN 1 x BEN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21212
Unit cell:
a: 79.886Å b: 63.19Å c: 50.313Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.283
Expression system: Spodoptera frugiperda

Quick links

Citations

3 review citations

Human plasma kallikrein-kinin system: physiological and biochemical parameters.
Bryant et al. (2009)
2 more

7 mentions without citation

The expanding diversity of serine hydrolases.
Botos et al. (2007)
6 more