1p11

X-ray diffraction
1.93Å resolution

CRYSTAL STRUCTURES OF ALPHA-LYTIC PROTEASE COMPLEXES WITH IRREVERSIBLY BOUND PHOSPHONATE ESTERS

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 trimer (preferred)
PDBe Complex ID:
PDB-CPX-133510 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Alpha-lytic protease Chain: E
Molecule details ›
Chain: E
Length: 198 amino acids
Theoretical weight: 19.88 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
PHOSPHONATE ESTER INHIBITOR A Chain: P
Molecule details ›
Chain: P
Length: 7 amino acids
Theoretical weight: 636 Da
Source organism: Lysobacter enzymogenes
Expression system: Not provided
PHOSPHONATE ESTER INHIBITOR B(TRANSITION STATE) Chain: I
Molecule details ›
Chain: I
Length: 5 amino acids
Theoretical weight: 493 Da
Source organism: Lysobacter enzymogenes
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 66.57Å b: 66.57Å c: 80.08Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.128 not available not available
Expression systems:
  • Escherichia coli
  • Not provided