› 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:
DOI: 10.2210/pdb1gbi/pdb
PDB entry 1gbi coloured by chain, front view.
PDB entry 1gbi coloured by chain, side view.
PDB entry 1gbi coloured by chain, top view.
Source organism: Lysobacter enzymogenes
Primary publication:
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
Mace JE, Agard DA
J Mol Biol 254 720-36 (1995)
PMID: 7500345

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133500 (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:
Ligand SO4 2 x SO4
1 modified residue:
Ligand B2F 1 x B2F

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

Quick links

Citations

1 review citation

Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold.
Perona et al. (1997)
20 other articles

1 mention without citation

Modeling and structural analysis of PA clan serine proteases.
Laskar et al. (2012)