› 3qh1

X-ray diffraction
1.55Å resolution

Structure of Thermolysin in complex with N-benzyloxycarbonyl-L-aspartic acid

Released:
DOI: 10.2210/pdb3qh1/pdb
PDB entry 3qh1 coloured by chain, front view.
PDB entry 3qh1 coloured by chain, side view.
PDB entry 3qh1 coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
Synthesis of Aspartame by Thermolysin: An X-ray Structural Study.
Birrane G, Bhyravbhatla B, Navia MA
ACS Med Chem Lett 5 706-10 (2014)
PMID: 24944748

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -|-Leu > -|-Phe.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermolysin Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 34.36 KDa
Source organism: Bacillus thermoproteolyticus
UniProt:
  • Canonical: P00800 (Residues: 233-548; Coverage: 61%)
Gene name: npr
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CA 4 x CA
Ligand ZN 1 x ZN
Ligand NX6 1 x NX6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P6122
Unit cell:
a: 92.503Å b: 92.503Å c: 130.102Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.115 0.113 0.15

Quick links

Citations

2 review citations

Amides in Nature and Biocatalysis.
Pitzer et al. (2016)
1 more

2 mentions without citation

Synthesis of Aspartame by Thermolysin: An X-ray Structural Study.
Birrane et al. (2014)
1 more