› 1p01

X-ray diffraction
2Å resolution

Serine protease mechanism. structure of an inhibitory complex oF ALPHA-LYTIC Protease and a tightly bound peptide boronic acid

Released:
DOI: 10.2210/pdb1p01/pdb
PDB entry 1p01 coloured by chain, front view.
PDB entry 1p01 coloured by chain, side view.
PDB entry 1p01 coloured by chain, top view.
Source organism: Lysobacter enzymogenes
Primary publication:
Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid.
Bone R, Shenvi AB, Kettner CA, Agard DA
Biochemistry 26 7609-14 (1987)
PMID: 3122831

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-lytic protease Chain: A
Molecule details ›
Chain: A
Length: 198 amino acids
Theoretical weight: 19.88 KDa
Source organism: Lysobacter enzymogenes
Expression system: Not provided
UniProt:
  • Canonical: P00778 (Residues: 200-397; Coverage: 53%)
Gene name: alpha-LP
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand 0EG 1 x 0EG
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 66.34Å b: 66.34Å c: 80.31Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.138 not available not available
Expression system: Not provided

Quick links

Citations

11 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
10 more

11 mentions without citation

Chemical shift-based methods in NMR structure determination.
Nerli et al. (2018)
10 more