› 1mzd

X-ray diffraction
2.9Å resolution

crystal structure of human pro-granzyme K

Released:
DOI: 10.2210/pdb1mzd/pdb
PDB entry 1mzd coloured by chain, front view.
PDB entry 1mzd coloured by chain, side view.
PDB entry 1mzd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 2.2-A crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual features.
Hink-Schauer C, Estébanez-Perpiñá E, Wilharm E, Fuentes-Prior P, Klinkert W, Bode W, Jenne DE
J Biol Chem 277 50923-33 (2002)
PMID: 12384499

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156069 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Granzyme K Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 26.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49863 (Residues: 25-264; Coverage: 100%)
Gene names: GZMK, TRYP2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 31.75Å b: 78.86Å c: 85.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.317
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases.
Korkmaz et al. (2010)
9 more

1 mention without citation

Allostery in trypsin-like proteases suggests new therapeutic strategies.
Gohara et al. (2011)