2ull

X-ray diffraction
1.5Å resolution

MULTIPLE CONFORMATION STRUCTURE OF ALPHA-LYTIC PROTEASE AT 120 K

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:
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: Escherichia coli
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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P3221
Unit cell:
a: 65.8Å b: 65.8Å c: 79.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.165 0.192
Expression system: Escherichia coli