› 1arc

X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb1arc/pdb
PDB entry 1arc coloured by chain, front view.
PDB entry 1arc coloured by chain, side view.
PDB entry 1arc coloured by chain, top view.
Source organism: Achromobacter lyticus
Primary publication:
The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease.
Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F
J Biol Chem 264 3832-9 (1989)
PMID: 2492988

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147412 (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

1 bound ligand:
Ligand TCK 1 x TCK
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 37.3Å b: 42.8Å c: 48Å
α: 120.1° β: 112.8° γ: 68.5°
R-values:
R R work R free
0.152 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Structural and energetic determinants of the S1-site specificity in serine proteases.
Czapinska et al. (1999)
2 more

3 mentions without citation

A comparative dosimetric study of left sided breast cancer after breast-conserving surgery treated with VMAT and IMRT.
Zhao et al. (2015)
2 more