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X-ray diffraction
1.3Å resolution

1.3A Structure of alpha-Lytic Protease Bound to Ac-AlaAlaPro-Alanal

Released:
Source organism: Lysobacter enzymogenes
Entry authors: Everill P, Meinke G, Bohm A, Bachovchin W

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

Assemblies composition:
hetero dimer (preferred)
hetero octamer
PDBe Complex ID:
PDB-CPX-133516 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-lytic protease Chains: A, C
Molecule details ›
Chains: A, C
Length: 198 amino acids
Theoretical weight: 19.88 KDa
Source organism: Lysobacter enzymogenes
UniProt:
  • Canonical: P00778 (Residues: 200-397; Coverage: 53%)
Gene name: alpha-LP
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ac-AlaAlaPro-Alanal peptide Chains: B, D
Molecule details ›
Chains: B, D
Length: 5 amino acids
Theoretical weight: 340 Da
Source organism: Lysobacter enzymogenes
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P6122
Unit cell:
a: 63.936Å b: 63.936Å c: 316.897Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.167 0.192
Expression system: Not provided