› 2qxg

X-ray diffraction
2.6Å resolution

Crystal Structure of Human Kallikrein 7 in Complex with Ala-Ala-Phe-chloromethylketone

Released:
DOI: 10.2210/pdb2qxg/pdb
PDB entry 2qxg coloured by chain, front view.
PDB entry 2qxg coloured by chain, side view.
PDB entry 2qxg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7.
Debela M, Hess P, Magdolen V, Schechter NM, Steiner T, Huber R, Bode W, Goettig P
Proc Natl Acad Sci U S A 104 16086-91 (2007)
PMID: 17909180

Function and Biology Details

Reaction catalysed: 
Cleavage of proteins with aromatic side chains in the P1 position
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kallikrein-7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 224 amino acids
Theoretical weight: 24.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49862 (Residues: 30-253; Coverage: 97%)
Gene names: KLK7, PRSS6, SCCE
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand K7I 2 x K7I
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 66.603Å b: 42.708Å c: 84.882Å
α: 90° β: 108.53° γ: 90°
R-values:
R R work R free
0.281 0.266 0.292
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Unleashing the therapeutic potential of human kallikrein-related serine proteases.
Prassas et al. (2015)
11 more

6 mentions without citation

Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).
Goettig et al. (2010)
5 more