› 4kga

X-ray diffraction
2.32Å resolution

Crystal structure of kallikrein-related peptidase 4

Released:
DOI: 10.2210/pdb4kga/pdb
PDB entry 4kga coloured by chain, front view.
PDB entry 4kga coloured by chain, side view.
PDB entry 4kga coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Direct and indirect mechanisms of KLK4 inhibition revealed by structure and dynamics.
Riley BT, Ilyichova O, Costa MG, Porebski BT, de Veer SJ, Swedberg JE, Kass I, Harris JM, Hoke DE, Buckle AM
Sci Rep 6 35385 (2016)
PMID: 27767076

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kallikrein-4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 23.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5K2 (Residues: 31-253; Coverage: 98%)
Gene names: EMSP1, KLK4, PRSS17, PSTS
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand NI 4 x NI
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P4
Unit cell:
a: 99.308Å b: 99.308Å c: 41.019Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.264
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

4 mentions without citation

Kallikreins - The melting pot of activity and function.
Kalinska et al. (2016)
3 more