› 2psx

X-ray diffraction
2.3Å resolution

Crystal Structure of Human Kallikrein 5 in complex with Leupeptin

Released:
DOI: 10.2210/pdb2psx/pdb
PDB entry 2psx coloured by chain, front view.
PDB entry 2psx coloured by chain, side view.
PDB entry 2psx coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis of the zinc inhibition of human tissue kallikrein 5.
Debela M, Goettig P, Magdolen V, Huber R, Schechter NM, Bode W
J Mol Biol 373 1017-31 (2007)
PMID: 17881000

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163179 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Kallikrein-5 Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 25.19 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9Y337 (Residues: 67-293; Coverage: 84%)
Gene names: KLK5, SCTE, UNQ570/PRO1132
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
LEUPEPTIN Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: Streptomyces roseus
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 125.219Å b: 67.284Å c: 39.916Å
α: 90° β: 94.35° γ: 90°
R-values:
R R work R free
0.244 0.221 0.269
Expression system: Not provided

Quick links

Citations

13 review citations

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

11 mentions without citation

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