› 5fah

X-ray diffraction
1.1Å resolution

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 Chain: A
Molecule details ›
Chain: A
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

2 bound ligands:
Ligand ACT 1 x ACT
Ligand 5VT 1 x 5VT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 42.611Å b: 60.343Å c: 80.633Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.196
Expression system: Escherichia coli

Quick links

Citations

17 review citations

The renaissance of complement therapeutics.
Ricklin et al. (2018)
16 more

1 mention without citation

An unexpected switch in peptide binding mode: from simulation to substrate specificity.
Kahler et al. (2018)