1gbi

X-ray diffraction
2.3Å resolution

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Ala-|-, Val-|- 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: 19.87 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-PHENYLALANINE BORONIC ACID INHIBITOR Chain: P
Molecule details ›
Chain: P
Length: 5 amino acids
Theoretical weight: 518 Da
Source organism: Lysobacter enzymogenes
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: 66.58Å b: 66.58Å c: 80.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.135 0.135 not available
Expression systems:
  • Escherichia coli
  • Not provided