PDBe 1arb

X-ray diffraction
1.2Å resolution

THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 1 Chain: A
Molecule details ›
Chain: A
Length: 268 amino acids
Theoretical weight: 27.76 KDa
Source organism: Achromobacter lyticus
Expression system: Not provided
UniProt:
  • Canonical: P15636 (Residues: 206-473; Coverage: 42%)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 39.54Å b: 40.36Å c: 43.93Å
α: 114.8° β: 113.73° γ: 74°
R-values:
R R work R free
0.149 not available not available
Expression system: Not provided