1qrw

X-ray diffraction
1.2Å resolution

CRYSTAL STRUCTURE OF AN ALPHA-LYTIC PROTEASE MUTANT WITH ACCELERATED FOLDING KINETICS, R102H/G134S, PH 8

Released:
Source organism: Lysobacter enzymogenes
Entry authors: Derman AI, Mau T, Agard DA

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-lytic protease Chain: A
Molecule details ›
Chain: A
Length: 198 amino acids
Theoretical weight: 19.89 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 BL9-1
Spacegroup: P3221
Unit cell:
a: 65.628Å b: 65.628Å c: 79.586Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.177 0.181
Expression system: Escherichia coli