PDBe 2lpr

X-ray diffraction
2.25Å resolution

STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-lytic protease Chain: A
Molecule details ›
Chain: A
Length: 198 amino acids
Theoretical weight: 19.82 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P00778 (Residues: 200-397; Coverage: 53%)
Gene name: alpha-LP
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
METHOXYSUCCINYL-ALA-ALA-PRO-VALINE BORONIC ACID INHIBITOR Chain: P
Molecule details ›
Chain: P
Length: 5 amino acids
Theoretical weight: 470 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 66.25Å b: 66.25Å c: 80.18Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.127 not available not available
Expression systems:
  • Escherichia coli
  • Not provided